CRYGD Mouse

Crystallin, Gamma D Mouse Recombinant
Cat. No.
BT20642
Source
Escherichia Coli.
Synonyms

Gamma-crystallin D, Gamma-D-crystallin , Gamma-crystallin 1, CRYGD.

Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% 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.
Shipped with Ice Packs
In Stock

Description

CRYGD Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids (1-174 a.a.) and having a molecular mass of 23.5kDa.
CRYGD is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
CRYGD, a member of the beta/gamma-crystallin family, is a structural component of the vertebrate eye lens. Mammalian lens crystallins are categorized into alpha, beta, and gamma families. Gamma-crystallins are implicated in cataract formation. Defects in the CRYGD gene are linked to various cataract types, including autosomal dominant (ADC), congenital non-nuclear polymorphic autosomal dominant (CCP), congenital cerulean type 3 (CCA3), and crystalline aculeiform (CACA).
Description
CRYGD Mouse Recombinant, produced in E.Coli, is a single, non-glycosylated polypeptide chain comprising 197 amino acids (1-174 a.a.) with a molecular mass of 23.5kDa. It is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Sterile filtered colorless solution.
Formulation
CRYGD protein solution at a concentration of 1mg/ml in 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), store at 4°C. For extended periods, store frozen at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity exceeds 95.0% as determined by SDS-PAGE.
Synonyms

Gamma-crystallin D, Gamma-D-crystallin , Gamma-crystallin 1, CRYGD.

Source
Escherichia Coli.
Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGSMGKITFY EDRGFQGRHY ECSTDHSNLQ PYFSRCNSVR VDSGCWMLYE QPNFTGCQYF LRRGDYPDYQ QWMGFSDSVR SCRLIPHAGS HRIRLYEREE YRGQMIEFTE DCPSLQDRFH FNEIYSLNVL EGCWVLYDMT NYRGRQYLLR PGEYRRYHDW
GAMNARVGSL RRVMDFY

Product Science Overview

Introduction

Crystallins are a family of proteins that are primarily found in the vertebrate eye lens, where they play a crucial role in maintaining the transparency and refractive index of the lens. Among the various types of crystallins, gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins that are typically devoid of connecting peptides and terminal extensions .

Structure and Function

Gamma-crystallin D (CRYGD) is one of the four gamma-crystallin genes (gamma-A through gamma-D) that are organized in a gene cluster. In mice, the CRYGD gene is located on chromosome 1 . The protein encoded by this gene is involved in maintaining the optical properties of the lens by ensuring its transparency and refractive power .

The mouse recombinant CRYGD protein is produced in E. coli and consists of a single, non-glycosylated polypeptide chain containing 197 amino acids (1-174 a.a.) with a molecular mass of 23.5 kDa. It is fused to a 23 amino acid His-tag at the N-terminus and purified using proprietary chromatographic techniques .

Biological Importance

Crystallins, including gamma-crystallins, are extremely stable proteins that are retained throughout the life of the lens cells. This stability is essential because lens central fiber cells lose their nuclei during development and do not produce or degrade proteins . The high concentration of crystallins in the lens helps to maintain its transparency and refractive index, which are critical for proper vision .

Role in Cataract Formation

Gamma-crystallins, including CRYGD, have been implicated in cataract formation. Cataracts are characterized by the clouding of the lens, which leads to a decrease in vision. This condition is often associated with the aggregation of crystallin proteins due to aging or mutations in specific genes . Understanding the structure and function of gamma-crystallins can provide insights into the mechanisms underlying cataract formation and potential therapeutic approaches.

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