gamma C Crystallin Antibody - BSA Free

Novus Biologicals | Catalog # NBP1-52908

Novus Biologicals
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Key Product Details

Species Reactivity

Human

Applications

Western Blot

Label

Unconjugated

Antibody Source

Polyclonal Rabbit IgG

Format

BSA Free
View all gamma C Crystallin Primary Antibodies »

Product Specifications

Immunogen

Synthetic peptides corresponding to CRYGC(crystallin, gamma C) The peptide sequence was selected from the middle region of CRYGC. Peptide sequence GLSDSIRSCCLIPQTVSHRLRLYEREDHKGLMMELSEDCPSIQDRFHLSE. The peptide sequence for this immunogen was taken from within the described region.

Clonality

Polyclonal

Host

Rabbit

Isotype

IgG

Theoretical MW

21 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Description

The addition of 50% glycerol is optional for those storing this antibody at -20C and not aliquoting smaller units. However, please note that glycerol may interrupt some downstream antibody applications and should be added with caution.

Scientific Data Images for gamma C Crystallin Antibody - BSA Free

Western Blot: gamma C Crystallin Antibody [NBP1-52908]

Western Blot: gamma C Crystallin Antibody [NBP1-52908]

Western Blot: gamma C Crystallin Antibody [NBP1-52908] - Titration: 0.2-1 ug/ml, Positive Control: OVCAR-3 cell lysate.

Applications for gamma C Crystallin Antibody - BSA Free

Application
Recommended Usage

Western Blot

1.0 ug/ml

Formulation, Preparation, and Storage

Purification

Affinity purified

Formulation

PBS, 2% Sucrose

Format

BSA Free

Preservative

0.09% Sodium Azide

Concentration

0.5 mg/ml

Shipping

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Stability & Storage

Store at 4C short term. Aliquot and store at -20C long term. Avoid freeze-thaw cycles.

Background: gamma C Crystallin

Crystallins are the dominant structural components of the vertebrate eye lens.Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Alternate Names

CCL, CRYG3gamma-C-crystallin, crystallin, gamma C, crystallin, gamma-3, Gamma-C-crystallin, Gamma-crystallin 2-1, Gamma-crystallin 3, gamma-crystallin C

Gene Symbol

CRYGC

UniProt

P07315 (Human)

Additional gamma C Crystallin Products

Product Documents for gamma C Crystallin Antibody - BSA Free

Certificate of Analysis

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Product Specific Notices for gamma C Crystallin Antibody - BSA Free

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

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