CRIP1 Human

Cysteine-Rich Protein 1 Human Recombinant
Cat. No.
BT25943
Source
Escherichia Coli.
Synonyms
Cysteine-rich protein 1, Cysteine-rich heart protein, CRHP, hCRHP, Cysteine-rich intestinal protein, CRIP, CRP1.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

CRIP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 100 amino acids (1-77 a.a) and having a molecular mass of 10.9kDa.
CRIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
CRIP1, also known as Cysteine-Rich Protein 1, is a member of the LIM/double zinc finger protein family. This family includes cysteine- and glycine-rich protein-1, rhombotin-1, rhombotin-2, and rhombotin-3. CRIP1 may be involved in zinc absorption and could function as an intracellular zinc transport protein. It has been associated with diseases like situs inversus and osteosarcoma.
Description
Recombinant human CRIP1 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 100 amino acids (residues 1-77), has a molecular weight of 10.9 kDa, and includes a 23 amino acid His-tag at the N-terminus. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
A clear, sterile-filtered solution.
Formulation
The CRIP1 protein solution is provided at a concentration of 0.25 mg/ml and contains 20mM Tris-HCl (pH 8.0), 20% glycerol, 0.15M NaCl, and 1mM DTT.
Stability
For short-term storage (up to 2-4 weeks), keep at 4°C. For longer 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 is greater than 95.0% as determined by SDS-PAGE analysis.
Synonyms
Cysteine-rich protein 1, Cysteine-rich heart protein, CRHP, hCRHP, Cysteine-rich intestinal protein, CRIP, CRP1.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPKCPKC NKEVYFAERV TSLGKDWHRP CLKCEKCGKT LTSGGHAEHE GKPYCNHPCY AAMFGPKGFG RGGAESHTFK

Product Science Overview

Gene and Protein Structure

CRIP1 is located on chromosome 14 at the band 14q32.33 . The protein is characterized by its high cysteine content and the presence of zinc finger motifs, which are crucial for its function in binding metal ions and DNA . The gene encoding CRIP1 is highly conserved across species, indicating its essential role in biological processes .

Biological Functions

CRIP1 is primarily involved in zinc absorption and may function as an intracellular zinc transport protein . Zinc is a vital trace element necessary for numerous biological functions, including enzyme activity, protein synthesis, and cell division. CRIP1’s role in zinc transport suggests its importance in maintaining cellular zinc homeostasis .

Additionally, CRIP1 has been implicated in various cellular processes such as:

  • Regulation of gene expression
  • Cellular response to antibiotics
  • Heart development
  • Immune response
  • Apoptotic signaling pathways in response to DNA damage
Clinical Significance

CRIP1 has been found to be expressed in several tumor types, including breast cancer . Its prognostic impact and role in tumorigenesis are subjects of ongoing research. Studies have shown that CRIP1 expression levels may correlate with tumor progression and patient outcomes, making it a potential biomarker for certain cancers .

Recombinant CRIP1

Recombinant CRIP1 refers to the protein produced through recombinant DNA technology, which involves inserting the CRIP1 gene into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. This recombinant protein can be used for various research purposes, including studying its structure, function, and potential therapeutic applications.

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