CRYGC Human

Crystallin, Gamma C Human Recombinant
Cat. No.
BT20464
Source
E.coli.
Synonyms
Crystallin, gamma C, Gamma-crystallin 2-1, Gamma-crystallin 3, CRYG3, CCL.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

CRYGC Human Recombinant produced in E. coli is a single polypeptide chain containing 198 amino acids (1-174) and having a molecular mass of 23.5kDa.
CRYGC is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
CRYGC, a member of the beta/gamma-crystallin family, plays a crucial role in maintaining lens transparency. Mammalian lens crystallins are categorized into alpha, beta, and gamma families, with beta and gamma crystallins often grouped as a superfamily. Gamma-crystallins, known for their high symmetry and monomeric structure, lack connecting peptides and terminal extensions. These proteins exhibit differential regulation after early development. The human genome contains a gene cluster encoding gamma-crystallins, consisting of three pseudogenes (gamma-E, F, G) and four functional genes (gamma-A, B, C, D). Mutations in CRYGC have been linked to cataract formation, specifically Coppock-like cataract (CCL) and autosomal dominant cataract (ADC).
Description
Recombinant human CRYGC, expressed in E. coli, is a single polypeptide chain with a molecular weight of 23.5 kDa. The protein comprises 198 amino acids, including a 24 amino acid His-tag at the N-terminus (1-174). Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterilized by filtration.
Formulation
CRYGC is supplied as a 1 mg/ml solution in 20mM Tris-HCl buffer (pH 8.0), 200mM NaCl, 2mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freezing and thawing should be avoided.
Purity
Purity is determined by SDS-PAGE analysis to be greater than 95%.
Synonyms
Crystallin, gamma C, Gamma-crystallin 2-1, Gamma-crystallin 3, CRYG3, CCL.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMGKITF YEDRAFQGRS YETTTDCPNL QPYFSRCNSI RVESGCWMLY ERPNYQGQQY LLRRGEYPDY QQWMGLSDSI RSCCLIPQTV SHRLRLYERE DHKGLMMELS EDCPSIQDRF HLSEIRSLHV LEGCWVLYEL PNYRGRQYLL RPQEYRRCQD WGAMDAKAGS LRRVVDLY

Product Science Overview

Gamma-Crystallin Family

Gamma-crystallins belong to the beta/gamma-crystallin superfamily, which also includes beta-crystallins. These proteins are differentially regulated after early development and are essential for the proper functioning of the lens . The human gamma-crystallin family includes several members, with Gamma C Crystallin (CRYGC) being one of them .

Structure and Expression

Recombinant Human Gamma C Crystallin is a full-length protein expressed in Escherichia coli with a purity greater than 95% . The protein sequence ranges from 1 to 174 amino acids and is suitable for applications such as SDS-PAGE and mass spectrometry . The structure of gamma-crystallins is highly conserved, which is critical for their function in the lens.

Function and Importance

Gamma-crystallins are essential for lens transparency and refractive properties. They fill the elongated, terminally differentiated fiber cells of the lens and must survive without turnover throughout life . Any mutations or changes in these proteins can lead to cataracts and loss of vision .

Evolutionary Perspective

The crystallin proteins have shown remarkable adaptation in different vertebrate lineages due to evolutionary pressures. Some crystallins have very restricted distributions among species, but the core set of alpha, beta, and gamma crystallins are widespread among vertebrates . These proteins have been recruited from existing proteins whose structure and properties suited them for the new role in the lens .

Applications

Recombinant Human Gamma C Crystallin is used in various research applications, including studies on protein structure, lens development, and cataract formation. Its high purity and expression in E. coli make it a valuable tool for scientific research .

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