Key Product Details

Species Reactivity

Validated:

Human

Cited:

Human, Mouse, Insect - Drosophila

Applications

Validated:

Western Blot, Intracellular Staining by Flow Cytometry, CyTOF-ready

Cited:

Immunohistochemistry, Immunohistochemistry-Paraffin, Western Blot, Immunocytochemistry, Simple Western

Label

Unconjugated

Antibody Source

Polyclonal Sheep IgG
View all Matriptase/ST14 Primary Antibodies »

Product Specifications

Immunogen

E. coli-derived recombinant human Matriptase/ST14 Catalytic Domain
Val615-Val855
Accession # Q9Y5Y6

Specificity

Detects human Matriptase/ST14 Catalytic Domain in direct ELISAs and Western blots.

Clonality

Polyclonal

Host

Sheep

Isotype

IgG

Scientific Data Images for Human Matriptase/ST14 Catalytic Domain Antibody

Detection of Matriptase/ST14 Catalytic Domain antibody in PC-3 Human Cell Line antibody by Flow Cytometry.

Detection of Matriptase/ST14 Catalytic Domain in PC‑3 Human Cell Line by Flow Cytometry.

PC-3 human prostate cancer cell line was stained with Sheep Anti-Human Matriptase/ST14 Catalytic Domain Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3946, filled histogram) or control antibody (5-001-A, open histogram), followed by NorthernLights™ 557-conjugated Anti-Sheep IgG Secondary Antibody (NL010). To facilitate intracellular staining, cells were fixed with paraformaldehyde and permeabilized with saponin.

Detection of Mouse Matriptase/ST14 by Simple Western

Detection of Mouse Matriptase/ST14 by Simple Western

Zymogen-locked matriptase induces epidermal prostasin processing. Protein extracts from skin (a), kidney (b), lung (c), and intestine (d) from newborn St14zym/zym (lanes 1 and 2), St14+/+ (lanes 3 and 4), and St14–/– (lane 5) littermates were separated by capillary electrophoresis and probed with antibodies against matriptase (top panels), prostasin (middle panels), or beta -actin (bottom panels). Lanes 6 and 7 in (a) are skin extracts from prostasin null (Prss8–/–) and prostasin zymogen-locked (Prss8zym/zym) mice, respectively. Zymogens of matriptase and prostasin are indicated with filled arrows, and the activated forms are indicated with open arrows. n.s. non-specific. Positions of molecular weight markers (kDa) are indicated on the left. e Representative example of quantification of activated prostasin (open arrow) and zymogen prostasin (filled arrows) in protein extracts from skin from a newborn St14zym/zym mouse (top panel), St14+/+ mouse (second panel from top), and a newborn St14–/– mouse (second panel from bottom). Skin extracts from a newborn mouse expressing zymogen-locked (Prss8zym/zym) endogenous prostasin is included as reference (bottom panel). f Ratio of activated prostasin to total prostasin in skin extracts from newborn St14zym/zym (left bar, n = 7), St14+/+ (middle bar, n = 7), and St14–/– (right bar, n = 2) mice, quantified as in (e). Data are shown as mean ± SD. *P = 0.0011 was determined by one-way ANOVA, two-tailed. Additional file 1: Raw supporting data Image collected and cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/28571576), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of Mouse Matriptase/ST14 by Simple Western

Detection of Mouse Matriptase/ST14 by Simple Western

Zymogen-locked matriptase induces epidermal prostasin processing. Protein extracts from skin (a), kidney (b), lung (c), and intestine (d) from newborn St14zym/zym (lanes 1 and 2), St14+/+ (lanes 3 and 4), and St14–/– (lane 5) littermates were separated by capillary electrophoresis and probed with antibodies against matriptase (top panels), prostasin (middle panels), or beta -actin (bottom panels). Lanes 6 and 7 in (a) are skin extracts from prostasin null (Prss8–/–) and prostasin zymogen-locked (Prss8zym/zym) mice, respectively. Zymogens of matriptase and prostasin are indicated with filled arrows, and the activated forms are indicated with open arrows. n.s. non-specific. Positions of molecular weight markers (kDa) are indicated on the left. e Representative example of quantification of activated prostasin (open arrow) and zymogen prostasin (filled arrows) in protein extracts from skin from a newborn St14zym/zym mouse (top panel), St14+/+ mouse (second panel from top), and a newborn St14–/– mouse (second panel from bottom). Skin extracts from a newborn mouse expressing zymogen-locked (Prss8zym/zym) endogenous prostasin is included as reference (bottom panel). f Ratio of activated prostasin to total prostasin in skin extracts from newborn St14zym/zym (left bar, n = 7), St14+/+ (middle bar, n = 7), and St14–/– (right bar, n = 2) mice, quantified as in (e). Data are shown as mean ± SD. *P = 0.0011 was determined by one-way ANOVA, two-tailed. Additional file 1: Raw supporting data Image collected and cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/28571576), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of Mouse Matriptase/ST14 by Simple Western

Detection of Mouse Matriptase/ST14 by Simple Western

Zymogen-locked matriptase induces epidermal prostasin processing. Protein extracts from skin (a), kidney (b), lung (c), and intestine (d) from newborn St14zym/zym (lanes 1 and 2), St14+/+ (lanes 3 and 4), and St14–/– (lane 5) littermates were separated by capillary electrophoresis and probed with antibodies against matriptase (top panels), prostasin (middle panels), or beta -actin (bottom panels). Lanes 6 and 7 in (a) are skin extracts from prostasin null (Prss8–/–) and prostasin zymogen-locked (Prss8zym/zym) mice, respectively. Zymogens of matriptase and prostasin are indicated with filled arrows, and the activated forms are indicated with open arrows. n.s. non-specific. Positions of molecular weight markers (kDa) are indicated on the left. e Representative example of quantification of activated prostasin (open arrow) and zymogen prostasin (filled arrows) in protein extracts from skin from a newborn St14zym/zym mouse (top panel), St14+/+ mouse (second panel from top), and a newborn St14–/– mouse (second panel from bottom). Skin extracts from a newborn mouse expressing zymogen-locked (Prss8zym/zym) endogenous prostasin is included as reference (bottom panel). f Ratio of activated prostasin to total prostasin in skin extracts from newborn St14zym/zym (left bar, n = 7), St14+/+ (middle bar, n = 7), and St14–/– (right bar, n = 2) mice, quantified as in (e). Data are shown as mean ± SD. *P = 0.0011 was determined by one-way ANOVA, two-tailed. Additional file 1: Raw supporting data Image collected and cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/28571576), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of Mouse Matriptase/ST14 by Simple Western

Detection of Mouse Matriptase/ST14 by Simple Western

Zymogen-locked matriptase induces epidermal prostasin processing. Protein extracts from skin (a), kidney (b), lung (c), and intestine (d) from newborn St14zym/zym (lanes 1 and 2), St14+/+ (lanes 3 and 4), and St14–/– (lane 5) littermates were separated by capillary electrophoresis and probed with antibodies against matriptase (top panels), prostasin (middle panels), or beta -actin (bottom panels). Lanes 6 and 7 in (a) are skin extracts from prostasin null (Prss8–/–) and prostasin zymogen-locked (Prss8zym/zym) mice, respectively. Zymogens of matriptase and prostasin are indicated with filled arrows, and the activated forms are indicated with open arrows. n.s. non-specific. Positions of molecular weight markers (kDa) are indicated on the left. e Representative example of quantification of activated prostasin (open arrow) and zymogen prostasin (filled arrows) in protein extracts from skin from a newborn St14zym/zym mouse (top panel), St14+/+ mouse (second panel from top), and a newborn St14–/– mouse (second panel from bottom). Skin extracts from a newborn mouse expressing zymogen-locked (Prss8zym/zym) endogenous prostasin is included as reference (bottom panel). f Ratio of activated prostasin to total prostasin in skin extracts from newborn St14zym/zym (left bar, n = 7), St14+/+ (middle bar, n = 7), and St14–/– (right bar, n = 2) mice, quantified as in (e). Data are shown as mean ± SD. *P = 0.0011 was determined by one-way ANOVA, two-tailed. Additional file 1: Raw supporting data Image collected and cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/28571576), licensed under a CC-BY license. Not internally tested by R&D Systems.
Detection of Mouse Matriptase/ST14 by Simple Western

Detection of Mouse Matriptase/ST14 by Simple Western

Zymogen-locked matriptase induces epidermal prostasin processing. Protein extracts from skin (a), kidney (b), lung (c), and intestine (d) from newborn St14zym/zym (lanes 1 and 2), St14+/+ (lanes 3 and 4), and St14–/– (lane 5) littermates were separated by capillary electrophoresis and probed with antibodies against matriptase (top panels), prostasin (middle panels), or beta -actin (bottom panels). Lanes 6 and 7 in (a) are skin extracts from prostasin null (Prss8–/–) and prostasin zymogen-locked (Prss8zym/zym) mice, respectively. Zymogens of matriptase and prostasin are indicated with filled arrows, and the activated forms are indicated with open arrows. n.s. non-specific. Positions of molecular weight markers (kDa) are indicated on the left. e Representative example of quantification of activated prostasin (open arrow) and zymogen prostasin (filled arrows) in protein extracts from skin from a newborn St14zym/zym mouse (top panel), St14+/+ mouse (second panel from top), and a newborn St14–/– mouse (second panel from bottom). Skin extracts from a newborn mouse expressing zymogen-locked (Prss8zym/zym) endogenous prostasin is included as reference (bottom panel). f Ratio of activated prostasin to total prostasin in skin extracts from newborn St14zym/zym (left bar, n = 7), St14+/+ (middle bar, n = 7), and St14–/– (right bar, n = 2) mice, quantified as in (e). Data are shown as mean ± SD. *P = 0.0011 was determined by one-way ANOVA, two-tailed. Additional file 1: Raw supporting data Image collected and cropped by CiteAb from the following publication (https://pubmed.ncbi.nlm.nih.gov/28571576), licensed under a CC-BY license. Not internally tested by R&D Systems.

Applications for Human Matriptase/ST14 Catalytic Domain Antibody

Application
Recommended Usage

CyTOF-ready

Ready to be labeled using established conjugation methods. No BSA or other carrier proteins that could interfere with conjugation.

Intracellular Staining by Flow Cytometry

2.5 µg/106 cells
Sample: PC‑3 human prostate cancer cell line fixed with paraformaldehyde and permeabilized with saponin

Western Blot

0.1 µg/mL
Sample: Recombinant Human Matriptase/ST14 Catalytic Domain

Reviewed Applications

Read 2 reviews rated 5 using AF3946 in the following applications:

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Advanced Features

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Flow Cytometry

Formulation, Preparation, and Storage

Purification

Antigen Affinity-purified

Reconstitution

Reconstitute at 0.2 mg/mL in sterile PBS. For liquid material, refer to CoA for concentration.

Formulation

Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.

Shipping

Lyophilized product is shipped at ambient temperature. Liquid small pack size (-SP) is shipped with polar packs. Upon receipt, store immediately at the temperature recommended below.

Stability & Storage

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 6 months, -20 to -70 °C under sterile conditions after reconstitution.

Calculators

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: Matriptase/ST14

Human matriptase, encoded by the ST14 (suppression of tumorogenicity 14) gene, is also known as tumor associated differentially expressed gene 15 protein/TADG‑15), epithin, and membrane-type serine protease 1/MT-SP1 (1). Predicted to have a significant role in tumor biology, matriptase may be a novel target for anti-cancer therapy (2). However, expressed in most human epithelia, matriptase is also important in several physiological processes (1). For example, it activates prostasin to initiate a protease cascade that is essential for epidermal differentiation (3), and it converts a single-chain IGFBP-rp1 into the two-chain form (4).

Matriptase is a type II transmembrane serine protease with a complex modular structure (1). The 855 amino acid (aa) sequence of human matriptase consists of a cytoplasmic tail (aa 1-55), a transmembrane domain (aa 56-76), and an extracellular portion (aa 77-855). The latter contains the following domains: SEA (aa 86-201), two CUBs (aa 214-334 and 340-447), four LDLRAs (aa 452-486, 487-523, 524-560, and 566-603), and a serine protease (aa 615-855). The physiological activation of the single-chain zymogen requires the cleavage at the SEA domain within the ER or Golgi, association with HAI-1, which facilitates the transport of the protease to the cell surface, and auto-cleavage at QAR-V(615)VGG (1). The activated matriptase is inhibited by HAI-1, and the resulting HAI-1 complex can be shed from the cell surface (1). R&D Systems rhST14 corresponds to the catalytic domain, and is inhibited effectively by rhHAI-1 and rhHAI-2A (R&D Systems, Catalog # 1048-PI and 1106-PI).

References

  1. List, K. et al. (2006) Mol. Med. 12:1.
  2. Uhland, K. (2006) Cell. Mol. Life Sci. 63:2968.
  3. Netzel-Arnett, S. et al. (2006) J. Biol. Chem. 281:32941.
  4. Ahmed, S. et al. (2006) FEBS J. 273:615.

Alternate Names

Epithin, MTSP1, PRSS14, SNC19, ST14, TADG-15, TMPRSS14

Entrez Gene IDs

6768 (Human); 19143 (Mouse); 114093 (Rat); 102117178 (Cynomolgus Monkey)

Gene Symbol

ST14

UniProt

Q9Y5Y6

Additional Matriptase/ST14 Products

Product Documents for Human Matriptase/ST14 Catalytic Domain Antibody

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Product Specific Notices for Human Matriptase/ST14 Catalytic Domain Antibody

For research use only

Citations for Human Matriptase/ST14 Catalytic Domain Antibody

Customer Reviews for Human Matriptase/ST14 Catalytic Domain Antibody (2)

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  • Human Matriptase/ST14 Catalytic Domain Antibody
    Name: Anonymous
    Application: Western Blot
    Sample Tested: Cell Lysates
    Species: E. coli
    Verified Customer | Posted 12/13/2019
    0.44 ug recombinant matriptase catalytic domain (R&D; Catalog Number: 3946-SEB) were used in a biochemical cleavage assay. Samples were analyzed under denaturing/reducing conditions by SDS-PAGE/western blot and stained using this matriptase catalytic domain antibody (0.1 ug/ml; blocking 1x supplemented with 10 % milk). I would recommend this antibody.
    Human Matriptase/ST14 Catalytic Domain Antibody AF3946
  • Human Matriptase/ST14 Catalytic Domain Antibody
    Name: Anonymous
    Application: Western Blot
    Sample Tested: S2 Drosophila embryonic epithelial cell line
    Species: Drosophila
    Verified Customer | Posted 12/11/2019
    Full length matriptase was overexpressed exclusively or co-overexpressed with its human inhibitor in Drosophila S2R+ cells. After three days incubation, supernatants of cells were examined under denaturing/reducing conditions using SDS-PAGE/western blot and antibody staining. The antibody stains three forms of matriptase: the mature and shedded matriptase as well as the catalytic domain.
    Human Matriptase/ST14 Catalytic Domain Antibody AF3946

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FAQs for Human Matriptase/ST14 Catalytic Domain Antibody

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  • Q: Why is intracellular flow staining performed with Human Matriptase/ST14 Catalytic Domain Antibody (Catalog #s MAB3946 and AF3946) when Human Matripase is a type II transmembrane serine protease?

    A: We have performed intracellular staining with Catalog #s MAB3946 and AF3946 because when PC-3 and some other cell lines were tested using the surface staining protocol, the results were negative. It is possible that the level of expression of this protein is too low to be detected on the surface. Furthermore, with optimization of staining, one may be able to detect protein on the surface.

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