SCGN Rat

Secretagogin Rat Recombinant
Cat. No.
BT19947
Source
Escherichia Coli.
Synonyms
SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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.
Shipped with Ice Packs
In Stock

Description

Secretagogin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 286 amino acids and having a molecular mass of 33.3 kDa.
The Rat SCGN is fused to a 10 a.a. His tag at N-Terminus.
The protein’s amino acids sequence is identical to UniProtKB/Swiss-Prot entry Q6R556.
The Rat SCGN is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Secretagogin (SCGN) is a calcium-binding protein found in the cytoplasm. It is related to calbindin D-28K and calretinin. SCGN is involved in potassium chloride-stimulated calcium flux and cell proliferation. It also plays a role in human non-functional pituitary adenomas.
Description
Recombinant Rat Secretagogin, produced in E. coli, is a single, non-glycosylated polypeptide chain containing 286 amino acids. It has a molecular mass of 33.3 kDa. The protein is fused to a 10 amino acid Histidine tag at the N-terminus. The amino acid sequence is identical to the UniProtKB/Swiss-Prot entry Q6R556. Rat SCGN is purified using proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The protein solution was sterile filtered, concentrated, and lyophilized with 20mM Tris and 50mM NaCl at pH 7.5.
Solubility
Reconstitute the lyophilized pellet in deionized water to a working concentration of 0.5 mg/ml. Allow the pellet to dissolve completely.
Stability
Store lyophilized protein at -20°C. After reconstitution, aliquot the protein to avoid repeated freeze/thaw cycles. Reconstituted protein can be stored at 4°C for a limited period.
Purity
Purity is determined to be greater than 95% by SDS-PAGE.
Synonyms
SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.
Source
Escherichia Coli.
Amino Acid Sequence
MKHHHHHHAS MDNAHRQTQA HLDAACFWQI WQRFDKDEKG YIKETELDAF FDDLLAKFGI EDTLMEENVQ KMKEQLMVGH DISKEGRILM KELASMFLSE DENFLLFFRL ETPLDNSVEF MQIWRKYDAD SSGFISAAEL SNFLRDLFLH HKKVISEAEL EEYTSTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DASSTEERKR DFEKIFAHYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCLGLKINP.

Product Science Overview

Discovery and Structure

Secretagogin was first identified and cloned as a novel member of the EF-hand family of calcium-binding proteins. The EF-hand motif is a helix-loop-helix structural domain that can bind calcium ions. Secretagogin contains six EF-hand motifs, which allow it to bind calcium with a relatively low affinity compared to other calcium-binding proteins like calbindin and calretinin .

Expression and Localization

Secretagogin is expressed in various tissues, but it is predominantly found in the central nervous system. In the rat, secretagogin is expressed in distinct neuron populations, including amacrine cells in the retina . These cells are interneurons located in the inner nuclear layer of the retina and play a crucial role in visual processing. Secretagogin-immunoreactive neurons in the retina have a relatively regular soma distribution and are involved in late-stage differentiation during neurogenesis .

Functional Role

The primary function of secretagogin is related to its ability to bind calcium ions. Calcium signaling is essential for various cellular processes, including neurotransmitter release, gene expression, and cell differentiation. Secretagogin’s role in calcium signaling suggests that it may be involved in regulating these processes in neurons. Additionally, secretagogin has been implicated in exocytosis, the process by which cells release substances, such as neurotransmitters, into the extracellular space .

Research and Applications

Research on secretagogin has provided valuable insights into its role in the nervous system. Studies have shown that secretagogin is involved in the development and function of specific neuron populations. For example, in the zebrafish retina, secretagogin-expressing amacrine cells have been characterized in both developmental and adult stages . This research forms the basis for functional studies assessing how the expression of distinct calcium-binding proteins might be regulated to compensate for the loss of one of the others .

In addition to its role in the nervous system, secretagogin has potential applications in biomedical research. Recombinant secretagogin, such as the rat recombinant form, is used in various experimental settings to study its function and interactions with other proteins. The availability of recombinant secretagogin allows researchers to investigate its properties in a controlled environment and develop potential therapeutic applications.

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