Search: 1000 results found for "GHRP"

Description:

Anti Human Leutenizing Hormone Paired Antibody Mouse

Product # :

ANT-787

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Description

Paired LH monoclonal antibodies are composed of anti-LH α and β subunits, the anti-LH α is used for the coating and antibody to β subunit is used for colloid gold conjugation. Please note that when ordering for example: 100µg paired antibody, you receive 50µg from each antibody (100µg in total).

Formulation

* LH α (Coating) antibody in 50mM NaCl, 10mM PBS, 0.1% NaN3, PH 8 (11.26mg/ml).
* LH β (Labeling) antibody in 50mM NaCl, 10mM PBS, 0.1% NaN3, PH 8 (18.39mg/ml).

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Physical Appearance
2 vials of sterile Filtered clear colorless solution.
Stability
For periods up to 1month LHPaired Antibody should be stored at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Applications
Lateral flow immunoassay.
Background
Luteinizing hormone (LH) is produced by the pituitary gland and takes an important part in the reproductive system. LH is necessary for sexual development and fertility in both males and females. In females, LH triggers ovulation and the production of progesterone. In males, LH stimulates testosterone production by the Leydig cells in the testes. LH testing can diagnose conditions related to excessive or insufficient LH production, such as infertility or pituitary gland disorders. LH takes an important part in the reproductive system, influencing sex hormone production, ovulation and in general reproductive function in both males and females.
Type
Mouse antibody Monoclonal.
Purification Method
Purified by Ion Exchange (IEX) Chromatography.

ProSpec'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.

Description:

Pregnancy-Associated Plasma Protein-1 Human

Pappalysin-1, Pregnancy-associated plasma protein A, PAPP-A, IGF-dependent IGFBP-4 protease, IGFBP-4ase, PAPPA, PAPA, DIPLA1, PAPPA1, ASBABP2.

Product # :

ENZ-1204

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Description

PAPP-A Human native purified from human placenta having a total molecular mass of ~200 kDa. The PAPP-A is purified by proprietary chromatographic techniques.

Source

Human Placenta

Formulation

PAPP-A protein was lyophilized from 10mM Tris-HCl pH-7, 0.15M NaCl, 0.1% NGME & 0.09% NaN3.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
PAPPA is a large zinc binding protein, which plays a role as a metalloprotease and specifically cleaves IGFBP-4 and IGFBP-5, resulting in release of bound IGF. PAPP-A regulates IGF bioactivity in various biological systems, including the human ovary and cardiovascular systems. PAPP A levels were higher in patients with unstable angina or acute myocardial infarction. PAPPA is also involved in local proliferative processes such as wound healing and bone remodeling. Moreover, PAPP-A is produced in high concentrations during pregnancy and is released into the maternal circulation. In placenta, PAPP A is expressed in X cells in septa and anchoring villi, and in syncytiotrophoblasts in the chorionic villi.
Synonyms
Pappalysin-1, Pregnancy-associated plasma protein A, PAPP-A, IGF-dependent IGFBP-4 protease, IGFBP-4ase, PAPPA, PAPA, DIPLA1, PAPPA1, ASBABP2.
Physical Appearance
Brownish lyophilized (freeze-dried) powder.
Stability
Lyophilized PAPP-A although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution PAPP-A should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Please prevent freeze-thaw cycles.
Solubility
It is recommended to add deionized water to a working concentration of 0.1mg/ml and let the lyophilized pellet dissolve completely.
Human Virus Test
Starting material tested and found negative for HIV-I, HIV-II, HCV antibodies and HBsAg antigen.

ProSpec'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.

Description:

Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO

BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen.

Product # :

CYT-1094

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Description

Bone Morphogenetic Protein Receptor-1A Human Recombinant produced in CHO cells is a glycosylated homodimer chain containing 2x362 amino acids and having a total molecular mass of 80.8kDa. BMPR1A is purified by proprietary chromatographic techniques.

Source

CHO cells.

Formulation

The protein was lyophilized from a sterile (0.2µm) filtered solution containing PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

The ED₅₀, as calculated by the Inhibition of human BMP-4-induced alkaline phosphatase production caused by ATDC5 cells is 120ng/ml corresponding to a specific activity of 8.3x10^3 units/mg.

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Introduction
The bone morphogenetic protein (BMP) receptors are a family of transmembrane serine/threonine kinases that include the type I receptors BMPR1A and BMPR1B and the type II receptor BMPR2. These receptors are also closely related to the receptors, ACVR1 and ACVR2. The ligands of these receptors are members of the TGF-beta superfamily. TGF-betas transduce their signals through the formation of heteromeric complexes with 2 different types of serine (threonine) kinase receptors: type I receptors of about 50-55 kD and type II receptors of about 70-80 kD. Type II receptors bind ligands in the absence of type I receptors, but they require their respective type I receptors for signaling, whereas type I receptors require their respective type II receptors for ligand binding.
Synonyms
BMPR-1A, BMP-R1A, BMPR1A, BMR1A, CD292, CD-292, Serine/threonine-protein kinase receptor R5, SKR5, ALK-3, ACVRLK3, EC 2.7.11.30, CD292 antigen.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BMPR1A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMPR1A should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized BMPR1A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
QNLDSMLHGT GMKSDSDQKK SENGVTLAPE DTLPFLKCYC SGHCPDDAIN NTCITNGHCF AIIEEDDQGE TTLASGCMKY EGSDFQCKDS PKAQLRRTIE CCRTNLCNQY LQPTLPPVVI GPFFDGSIRI EGRMDDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK.
Background
Research Paper on Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO, Monomer, HEK
Abstract:
Welcome to the captivating world of Bone Morphogenetic Protein Receptor-1A Human Recombinant, CHO, Monomer (BMPR-1A HR) in Human Embryonic Kidney Cells (HEK). This research paper explores the vital role of BMPR-1A HR in cellular responses. As a key receptor in the transforming growth factor-beta (TGF-β) superfamily, BMPR-1A HR plays a significant part in guiding cellular differentiation and tissue development. Join us as we unravel the molecular mechanisms behind BMPR-1A HR signaling in HEK cells and delve into its interactions with key cytokines, including Tumor Necrosis Factor-alpha (TNF-α) and Tumor Necrosis Factor-alpha Superfamily Member 2 (TNFα SF2 or TNFSF2).
Introduction:
Welcome to the intriguing world of BMPR-1A HR! In this section, we introduce the remarkable BMPR-1A HR and its crucial role in shaping cellular responses. Together, let's explore how this receptor influences cellular behavior and contributes to tissue growth, fostering our understanding of its importance in biological processes.
BMPR-1A HR Signaling in HEK Cells:
Be amazed by the intricate dance of BMPR-1A HR signaling within HEK cells! Uncover the complex process of ligand-receptor binding, initiating both the canonical SMAD-dependent and non-canonical SMAD-independent pathways. This harmonious interplay regulates a wide range of cellular processes, including gene transcription, cell proliferation, and differentiation, forming the foundation of cellular communication.
Influential Role in Cellular Responses:
Marvel at the influential role of BMPR-1A HR as a critical mediator of cellular responses within HEK cells. Witness its ability to modulate cellular differentiation, driving the expression of key differentiation markers such as DIF. Our exploration will highlight the multifaceted nature of BMPR-1A HR, impacting diverse cellular pathways, including those involving TNF-α and TNFSF2, shaping a dynamic and interconnected cellular network.
Interplay with Key Cytokines:
Discover the intriguing interactions between BMPR-1A HR and key cytokines like TNF-α and TNFSF2. Explore how BMPR-1A HR influences their expression and activity, hinting at potential cross-talk between BMPR-1A HR and inflammatory pathways. This delicate balance fosters a harmonious cellular environment, where multiple players contribute to overall cellular responses.
Therapeutic Implications and Tissue Development:
Witness the potential therapeutic implications of BMPR-1A HR in tissue development. Together, we explore the exciting possibilities of utilizing BMPR-1A HR in regenerative medicine, offering hope for enhanced tissue development and repair. As we venture forth, we also address challenges, such as optimal dosage, innovative delivery methods, and safety considerations, ensuring a responsible and effective approach.
Conclusion:
As we conclude our exploration of BMPR-1A HR in HEK cells, we stand in awe of its role in mediating cellular responses and tissue development. Equipped with this knowledge, we look forward to a promising future, where BMPR-1A HR from CHO cells opens doors to innovative applications in regenerative medicine, contributing to improved human health and well-being.
What is the molecular weight/Mw of BMPR1A Protein?
BMPR1A Protein has a total Mw of 80.8kDa.

What is the source or expression system of BMPR1A Protein?
CHO cells.

What is the Purity of BMPR1A Protein?
BMPR1A Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of BMPR1A Protein?
The ED50, as calculated by the Inhibition of human BMP-4-induced alkaline phosphatase production caused by ATDC5 cells is 120ng/ml corresponding to a specific activity of 8.3x10^3 units/mg.

What is the amino acid sequence of BMPR1A Protein?
QNLDSMLHGT GMKSDSDQKK SENGVTLAPE DTLPFLKCYC SGHCPDDAIN NTCITNGHCF AIIEEDDQGE TTLASGCMKY EGSDFQCKDS PKAQLRRTIE CCRTNLCNQY LQPTLPPVVI GPFFDGSIRI EGRMDDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GK.

What applications can BMPR1A Protein be used in?
BMPR1A Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for BMPR1A Protein?
The endotoxin level is minimal, BMPR1A Protein was purified using conventional chromatography techniques.

ProSpec'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.

Description:

GTPase Activating Protein (SH3 domain) Binding Protein 1 Human Recombinant

Ras GTPase-activating protein-binding protein 1, G3BP-1, ATP-dependent DNA helicase VIII, hDH VIII, GAP SH3 domain-binding protein 1, G3BP1, G3BP, HDH-VIII, MGC111040.

Product # :

ENZ-048

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Description

G3BP1 Human Recombinant fused with an 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 474 amino acids (1-466 a.a.) and having a molecular mass of 53.2kDa.The G3BP1 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The G3BP1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 100mM NaCl.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
G3BP1 belongs to the heterogeneous nuclear RNA-binding proteins and is also an element of the Ras signal transduction pathway. G3BP1 is one of the DNA-unwinding enzymes that favors partially unwound 3'-tailed substrates and is also able to unwind partial RNA/DNA and RNA/RNA duplexes in an ATP-dependent fashion. G3BP1 binds specifically to the Ras-GTPase-activating protein by associating with its SH3 domain. In addition, G3BP1 cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR.
Synonyms
Ras GTPase-activating protein-binding protein 1, G3BP-1, ATP-dependent DNA helicase VIII, hDH VIII, GAP SH3 domain-binding protein 1, G3BP1, G3BP, HDH-VIII, MGC111040.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MVMEKPSPLL VGREFVRQYY TLLNQAPDML HRFYGKNSSY VHGGLDSNGK PADAVYGQKE IHRKVMSQNF TNCHTKIRHV DAHATLNDGV VVQVMGLLSN NNQALRRFMQ TFVLAPEGSV ANKFYVHNDI FRYQDEVFGG FVTEPQEESE EEVEEPEERQ QTPEVVPDDS GTFYDQAVVS NDMEEHLEEP VAEPEPDPEP EPEQEPVSEI QEEKPEPVLE ETAPEDAQKS SSPAPADIAQ TVQEDLRTFS WASVTSKNLP PSGAVPVTGI PPHVVKVPAS QPRPESKPES QIPPQRPQRD QRVREQRINI PPQRGPRPIR EAGEQGDIEP RRMVRHPDSH QLFIGNLPHE VDKSELKDFF QSYGNVVELR INSGGKLPNF GFVVFDDSEP VQKVLSNRPI MFRGEVRLNV EEKKTRAARE GDRRDNRLRG PGGPRGGLGG GMRGPPRGGM VQKPGFGVGR GLAPRQVEHH HHHH.

ProSpec'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.

Description:

Protease Serine 3 Human Recombinant, HEK

Protease, Serine, 3, Protease, Serine, 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Mesotrypsin, Trypsin III, EC 3.4.21.4 4, Trypsin IV, PRSS4, TRY3, TRY4 Protease, Serine, 3 (Mesotrypsin), Pancreatic Trypsinogen III, Serine Protease 3, Serine Protease 4, Trypsinogen IV, Trypsinogen 4, Trypsinogen 5, EC 3.4.21, MTG, T9.

Product # :

ENZ-1194

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Description

PRSS3 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 238 amino acids (16-247 a.a.) and having a molecular mass of 26kDa. PRSS3 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

PRSS3 protein solution (1mg/ml) containing 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 10,000pmol/min/ug, and is defined as the amount of enzyme that cleaves 1pmol of McaRPKPVE-Nval-WRK(Dnp)-NH2 per minute at pH 8.0 at 37℃.

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Synonyms
Protease, Serine, 3, Protease, Serine, 4 (Trypsin 4, Brain), Brain Trypsinogen, Mesotrypsinogen, Mesotrypsin, Trypsin III, EC 3.4.21.4 4, Trypsin IV, PRSS4, TRY3, TRY4 Protease, Serine, 3 (Mesotrypsin), Pancreatic Trypsinogen III, Serine Protease 3, Serine Protease 4, Trypsinogen IV, Trypsinogen 4, Trypsinogen 5, EC 3.4.21, MTG, T9.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
VPFDDDDKIV GGYTCEENSL PYQVSLNSGS HFCGGSLISE QWVVSAAHCY KTRIQVRLGE HNIKVLEGNE QFINAAKIIR HPKYNRDTLD NDIMLIKLSS PAVINARVST ISLPTAPPAA GTECLISGWG NTLSFGADYP DELKCLDAPV LTQAECKASY PGKITNSMFC VGFLEGGKDS CQRDSGGPVV CNGQLQGVVS WGHGCAWKNR PGVYTKVYNY VDWIKDTIAA NSHHHHHH.
Background
PRSS3 is a member of the serine protease family, characterized by its specific enzymatic activity mediated by the serine residue in the catalytic triad. PRSS3's structure consists of a catalytic domain, a substrate-binding site, and disulfide bridges that help maintain its stability. Understanding the molecular characteristics of PRSS3 is crucial for elucidating its functions.
Physiological Functions: PRSS3 is primarily expressed in the pancreas, where it plays a vital role in the digestion of dietary proteins. It contributes to the breakdown of proteins into smaller peptides, facilitating their absorption in the small intestine. PRSS3 is part of a complex enzymatic network that ensures proper digestion and nutrient absorption.
Pathological Implications: Research has shown that abnormal PRSS3 activity or expression can be associated with various diseases. For example, alterations in PRSS3 have been linked to pancreatic diseases, including pancreatitis and pancreatic cancer. Investigating PRSS3's role in disease pathogenesis can provide valuable insights into the development and progression of these conditions.
Biomedical Research: PRSS3 human recombinant proteins are valuable tools in biomedical research. Researchers use these recombinant proteins to study PRSS3's enzymatic properties, interactions with other molecules, and potential therapeutic applications. They can perform controlled experiments to gain a deeper understanding of PRSS3's functions.
Therapeutic Potential: PRSS3's involvement in diseases like pancreatitis and pancreatic cancer has raised interest in its therapeutic potential. Researchers explore the development of inhibitors or modulators targeting PRSS3 as potential treatments for these diseases. Additionally, PRSS3's role in protein digestion has implications for digestive disorders and enzyme replacement therapies.
Diagnostic Markers: PRSS3 levels or activity may serve as diagnostic markers for certain diseases. Changes in PRSS3 expression in pancreatic tissue or serum may be indicative of pancreatic disorders. Research in this area aims to establish PRSS3 as a diagnostic tool for early disease detection.
Future Directions: Continued research on PRSS3 human recombinant and its roles in health and disease is essential. This includes investigating its regulation, substrate specificity, and potential interactions with other proteins. Such studies may uncover novel therapeutic targets and diagnostic strategies.

ProSpec'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.

Description:

Histidyl-tRNA Synthetase Human Recombinant, His Tag

Histidyl-tRNA synthetase cytoplasmic, Histidine--tRNA ligase, HisRS, HARS, HRS, FLJ20491.

Product # :

ENZ-001

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Description

HARS Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 532 amino acids (1-509 a.a.) and having a molecular mass of 59.4kDa. The HARS is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HARS solution (1mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol,
1mM DTT and 0.1M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Histidyl-tRNA synthetase (HARS) functions to catalyze the aminoacylation of tRNAs by their corresponding amino acids. HARS is a member of the class II family of aminoacyl-tRNA synthetases. HARS is responsible for the synthesis of histidyl-transfer RNA, which is vital for the incorporation of histidine into proteins. HARS is a frequent target of autoantibodies in the human autoimmune disease polymyositis/dermatomyositis.
Synonyms
Histidyl-tRNA synthetase cytoplasmic, Histidine--tRNA ligase, HisRS, HARS, HRS, FLJ20491.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAERAAL EELVKLQGER VRGLKQQKAS AELIEEEVAK LLKLKAQLGP DESKQKFVLK TPKGTRDYSP RQMAVREKVF DVIIRCFKRH GAEVIDTPVF ELKETLMGKY GEDSKLIYDL KDQGGELLSL RYDLTVPFAR YLAMNKLTNI KRYHIAKVYR RDNPAMTRGR YREFYQCDFD IAGNFDPMIP DAECLKIMCE ILSSLQIGDF LVKVNDRRIL DGMFAICGVS DSKFRTICSS VDKLDKVSWE EVKNEMVGEK GLAPEVADRI GDYVQQHGGV SLVEQLLQDP KLSQNKQALE GLGDLKLLFE YLTLFGIDDK ISFDLSLARG LDYYTGVIYE AVLLQTPAQA GEEPLGVGSV AAGGRYDGLV GMFDPKGRKV PCVGLSIGVE RIFSIVEQRL EALEEKIRTT ETQVLVASAQ KKLLEERLKL VSELWDAGIK AELLYKKNPK LLNQLQYCEE AGIPLVAIIG EQELKDGVIK LRSVTSREEV DVRREDLVEE IKRRTGQPLC IC.

ProSpec'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.

Description:

Growth and Differentiation factor 7 Mouse Recombinant

Growth/differentiation factor 7, GDF-7, Gdf7.

Product # :

CYT-946

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Description

GDF7 Mouse Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 146 amino acids and having a molecular mass of 29.8kDa.The GDF-7 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GDF7 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

Purity

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 0.5µg/ml, corresponding to a specific activity of > 2000 IU/mg.

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Introduction
Growth Differentiation Factor-7 (GDF-7) belongs to the BMP family of TGF-b superfamily proteins. GDF7 elicits its bioactivity via a heterodimeric receptor complex comprised of a type 1 (BMPR-IB) and a type II (BMPR-II or Activin RII) serine/threonine kinase receptor. GDF7 signaling results in the phosphorylation and activation of Smad proteins. GDF-7 is also involved in tendon and ligament formation and repair. In addition, GDF7 regulates bone formation, mesenchymal stem cell differentiation, neuronal differentiation, and axon guidance.
Synonyms
Growth/differentiation factor 7, GDF-7, Gdf7.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GDF7 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GDF-7 should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GDF-7 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TALAGTRGAQ GSGGGGGGGG GGGGGGGGGG GGAGRGHGRR GRSRCSRKSL HVDFKELGWD DWIIAPLDYE AYHCEGVCDF PLRSHLEPTN HAIIQTLLNS MAPDAAPASC CVPARLSPIS ILYIDAANNV VYKQYEDMVV EACGCR.
Background
What is the molecular weight/Mw of GDF7 Protein?
GDF7 Protein has a total Mw of 29.8kDa.

What is the source or expression system of GDF7 Protein?
Escherichia Coli.

What is the Purity of GDF7 Protein?
GDF7 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF7 Protein?
The ED50 as determined by inducing alkaline phosphatase production of murine ATDC5 cells is less than 0.5µg/ml, corresponding to a specific activity of > 2000 IU/mg.

What is the amino acid sequence of GDF7 Protein?
TALAGTRGAQ GSGGGGGGGG GGGGGGGGGG GGAGRGHGRR GRSRCSRKSL HVDFKELGWD DWIIAPLDYE AYHCEGVCDF PLRSHLEPTN HAIIQTLLNS MAPDAAPASC CVPARLSPIS ILYIDAANNV VYKQYEDMVV EACGCR.

What applications can GDF7 Protein be used in?
GDF7 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF7 Protein?
The endotoxin level is minimal, GDF7 Protein was purified using conventional chromatography techniques.

ProSpec'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.

Description:

Adipogenesis Associated, Mth938 Domain Containing Human Recombinant

Adipogenesis Associated, Mth938 Domain Containing, Adipogenesis Associated Mth938 Domain-Containing Protein , C11orf67, Chromosome 11 Open Reading Frame 67, Mth938 Domain-Containing Protein, UPF0366 Protein C11orf67, PTD015, CK067,AAMDC.

Product # :

PRO-2116

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Description

AAMDC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 145 amino acids (1-122 a.a) and having a molecular mass of 15.7 kDa.AAMDC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

AAMDC protein solution (1mg/ml) containing Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Adipogenesis Associated, Mth938 Domain Containing, also known as AAMDC is a member of the AAMDC family and takes part in preadipocyte differentiation andadipogenesis.
Synonyms
Adipogenesis Associated, Mth938 Domain Containing, Adipogenesis Associated Mth938 Domain-Containing Protein , C11orf67, Chromosome 11 Open Reading Frame 67, Mth938 Domain-Containing Protein, UPF0366 Protein C11orf67, PTD015, CK067,AAMDC.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTSPEIA SLSWGQMKVK GSNTTYKDCK VWPGGSRTWD WRETGTEHSP GVQPADVKEV VEKGVQTLVI GRGMSEALKV PSSTVEYLKK HGIDVRVLQT EQAVKEYNAL VAQGVRVGGV FHSTC.

ProSpec'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.

Description:

GM-CSF Receptor Alpha Human Recombinant

CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.

Product # :

CYT-796

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Description

CSF2RA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (20-320 a.a) and having a molecular mass of 37.2kDa.CSF2RA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CSF2RA protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
GM-CSF Receptor Alpha (CSF2RA) is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. CSFR2 is also a member of the cytokine family of receptors. In addition, this gene is found in the pseudoautosomal region (PAR) of the X and Y chromosomes. Multiple transcript variants encoding various isoforms have been found for this gene, while some of the isoforms being membrane-bound and others being soluble. Diseases associated with CSF2RA include surfactant metabolism dysfunction, pulmonary 4, and csf2ra-related pulmonary surfactant metabolism dysfunction.
Synonyms
CD116, CDw116, CSF2R, GM-CSF-R-alpha, GMCSFR, GMR, SMDP4, GMR-alpha, CD116 Antigen, CSF2RAX, CSF2RY, CSF2RAY, CSF2RX, Colony Stimulating Factor 2 Receptor Alpha Subunit, GM-CSF Receptor Alpha Subunit, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Alpha Chain, Granulocyte-Macrophage Colony-Stimulating Factor Receptor Subunit Alpha.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Background
Unlocking the Potential of Human Recombinant Ciliary Neurotrophic Factor Receptor: Implications and Applications
Abstract:
The Ciliary Neurotrophic Factor Receptor (CNTFR) plays a pivotal role in mediating the effects of ciliary neurotrophic factor (CNTF) on neuronal survival and growth. This paper examines the significance of Human Recombinant CNTFR, its production techniques, and its potential applications in neurobiology and therapeutic interventions. The review underscores CNTFR's crucial role in advancing neuroprotection and neuroregeneration research.
Introduction:
CNTFR, a transmembrane protein, is central to transducing the signals initiated by CNTF. Availability of Human Recombinant CNTFR enables researchers to dissect its contribution to neuronal function and develop targeted therapies for neurodegenerative disorders. CNTFR's role in modulating neuronal health and promoting regeneration makes it a cornerstone in neurobiology.
Role in CNTF Signaling:
CNTFR forms a receptor complex with other proteins, including gp130 and LIFRβ, to bind CNTF and trigger downstream signaling pathways. Activation of intracellular cascades, such as JAK/STAT and MAPK, is instrumental in driving the neuroprotective and growth-promoting effects of CNTF.
Production Methods:
Human Recombinant CNTFR is generated through gene expression in suitable host cells, often utilizing bacterial or mammalian systems. Ensuring accurate folding and post-translational modifications is crucial to preserve its functionality and affinity for CNTF.
Therapeutic Applications:
Human Recombinant CNTFR holds promise for therapeutic applications in neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), multiple sclerosis, and retinal degeneration. Manipulating CNTFR-associated signaling presents opportunities to bolster neuronal survival and regeneration, potentially revolutionizing patient care.
Challenges and Future Directions:
While the potential is significant, challenges encompass optimizing CNTFR-CNTF interactions, effective tissue delivery, and understanding potential off-target effects. Ongoing research is paramount to unravel the complete mechanisms of CNTFR-mediated signaling and its therapeutic implications.
Conclusion:
Human Recombinant Ciliary Neurotrophic Factor Receptor emerges as a vital tool in advancing our grasp of neuroprotection and regeneration. Its capacity to modulate CNTF effects opens doors to innovative therapeutic strategies for addressing neurodegenerative disorders, embodying the intersection of molecular insights and clinical progress.
What is the molecular weight/Mw of CD116 Protein?
CD116 Protein has a total Mw of 37.2kDa.

What is the source or expression system of CD116 Protein?
Escherichia Coli.

What is the Purity of CD116 Protein?
CD116 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of CD116 Protein?
The biological functionality of CD116 Protein will be determined in the future.

What is the amino acid sequence of CD116 Protein?
CD116 Protein is composed from 324 amino acids.

What applications can CD116 Protein be used in?
CD116 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD116 Protein?
The endotoxin level is minimal, CD116 Protein was purified using conventional chromatography techniques.

ProSpec'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.

Description:

Cyclophilin-D Human Recombinant, His Tag

Peptidylprolyl isomerase D, PPID, CYPD, CYP-40, 40 kDa peptidyl-prolyl cis-trans isomerase, PPIase, Rotamase, Cyclophilin-40, CYP40, Cyclophilin-related protein, MGC33096, EC 5.2.1.8.

Product # :

ENZ-367

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Description

Cyclophilin-D Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (amino acids 1-370) containing 390 amino acids and having a molecular mass of 42.9kDa. Cyclophilin-D is fused to a 20 aa His Tag at N-terminus and is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

1mg/ml solution containing 1x PBS pH-7.4 & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 700 nmol/min/mg, and is defined as the amount of enzyme that cleaves 1nmole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

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Introduction
Cyclophilin-D is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and speeds up the protein folding. Cyclophilin-D possess PPIase activity and binds to the immunosuppressant cyclosporin-A. Cyclophilin-D is very well known that its overexpression suppresses the apoptosis in cancer cell. Cyclophilin-D suppresses apoptotic cell death by the use of mitochondrial hexokinase-2 dependent mechanism in cancer cells.
Synonyms
Peptidylprolyl isomerase D, PPID, CYPD, CYP-40, 40 kDa peptidyl-prolyl cis-trans isomerase, PPIase, Rotamase, Cyclophilin-40, CYP40, Cyclophilin-related protein, MGC33096, EC 5.2.1.8.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSHPSPQAKP SNPSNPRVFFDVDIGGERVG RIVLELFADI VPKTAENFRA LCTGEKGIGH TTGKPLHFKG CPFHRIIKKF MIQGGDFSNQ NGTGGESIYG EKFEDENFHY KHDREGLLSMANAGRNTNGS QFFITTVPTP HLDGKHVVFG QVIKGIGVAR ILENVEVKGEKPAKLCVIAE CGELKEGDDG GIFPKDGSGD SHPDFPEDAD IDLKDVDKIL LITEDLKNIG NTFFKSQNWE MAIKKYAEVL RYVDSSKAVI ETADRAKLQPIALSCVLNIG ACKLKMSNWQ GAIDSCLEAL ELDPSNTKAL YRRAQGWQGLKEYDQALADL KKAQGIAPED KAIQAELLKV KQKIKAQKDK EKAVYAKMFA.

ProSpec'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.

Description:

Major Histocompatibility Complex Class I C Human Recombinant

Major Histocompatibility Complex Class I- C, D6S204, HLA-JY3, PSORS1, HLC-C, HLA Class I Histocompatibility Antigen C Alpha Chain, Human Leukocyte Antigen-C Alpha Chain, Major Histocompatibility Antigen HLA-C, MHC Class I Antigen Heavy Chain HLA-C.

Product # :

PRO-1562

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Description

HLA-C Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 307 amino acids (25-308) and having a molecular mass of 34.9kDa.HLA-C is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HLA-C solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Major Histocompatibility Complex Class I C (HLA-C) belongs to the HLA class I heavy chain paralogues. The HLA-C (class I molecule) is a heterodimer comprised of a heavy chain and a light chain (beta-2 microglobulin). The heavy chain is anchored in the membrane. Class I molecules have a key role in the immune system by presenting peptides derived from endoplasmic reticulum lumen. Class I molecules are expressed in virtually all cells.
Synonyms
Major Histocompatibility Complex Class I- C, D6S204, HLA-JY3, PSORS1, HLC-C, HLA Class I Histocompatibility Antigen C Alpha Chain, Human Leukocyte Antigen-C Alpha Chain, Major Histocompatibility Antigen HLA-C, MHC Class I Antigen Heavy Chain HLA-C.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSCSHSMRY FDTAVSRPGR GEPRFISVGY VDDTQFVRFD SDAASPRGEP RAPWVEQEGP EYWDRETQKY KRQAQADRVS LRNLRGYYNQ SEDGSHTLQR MSGCDLGPDG RLLRGYDQSA YDGKDYIALN EDLRSWTAAD TAAQITQRKL EAARAAEQLR AYLEGTCVEW LRRYLENGKE TLQRAEPPKT HVTHHPLSDH EATLRCWALG FYPAEITLTW QRDGEDQTQD TELVETRPAG DGTFQKWAAV VVPSGQEQRY TCHMQHEGLQ EPLTLSWEPS SQPTIPI

ProSpec'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.

Description:

B-Raf Proto-Oncogene Human Recombinant

Proto-Oncogene B-Raf, BRAF1, RAFB1, NS7, EC 2.7.11.1, B-RAF1, P94.

Product # :

PKA-071

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Description

BRAF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 360 amino acids (432-766a.a) and having a molecular mass of 40.6kDa. BRAF is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BRAF protein solution (0.25mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 80.0% as determined by SDS-PAGE.

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Introduction
B-Raf Proto-Oncogene, also known as BRAF is a member of the raf/mil family of serine/threonine protein kinases. BRAF participates in regulating the MAP kinase/ERKs signaling pathway, which eventually have an effect on cell division, differentiation, and secretion. Mutations in BRAF have been associated with cardiofaciocutaneous syndrome, which is a disease characterized by heart defects, mental retardation and a distinctive facial appearance. In addition, mutations in BRAF have also been associated with different cancers, including non-Hodgkin lymphoma, colorectal cancer, malignant melanoma, thyroid carcinoma, non-small cell lung carcinoma, as well as adenocarcinoma of lung.
Synonyms
Proto-Oncogene B-Raf, BRAF1, RAFB1, NS7, EC 2.7.11.1, B-RAF1, P94.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSEFSEDRN RMKTLGRRDS SDDWEIPDGQ ITVGQRIGSG SFGTVYKGKW HGDVAVKMLN VTAPTPQQLQ AFKNEVGVLR KTRHVNILLF MGYSTKPQLA IVTQWCEGSS LYHHLHIIET KFEMIKLIDI ARQTAQGMDY LHAKSIIHRD LKSNNIFLHE DLTVKIGDFG LATVKSRWSG SHQFEQLSGS ILWMAPEVIR MQDKNPYSFQ SDVYAFGIVL YELMTGQLPY SNINNRDQII FMVGRGYLSP DLSKVRSNCP KAMKRLMAEC LKKKRDERPL FPQILASIEL LARSLPKIHR SASEPSLNRA GFQTEDFSLY ACASPKTPIQ AGGYGAFPVH.

ProSpec'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.

Description:

Fibroblast Growth Factor-basic Human Recombinant, Thermostable

HBGH-2, HBGF-2, FGF-2, FGF-b, HBGH2, HBGF2, FGF2, FGFb, FGF2 Thermostable, FGF-2 Thermostable.

Product # :

CYT-943

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Description

FGF2 Thermostable is a stabilized form of FGF2 growth factor which enables a novel method to produce FGF2-dependent cell cultures more efficiently, having less media changes. FGF2 Thermostable can maintain its biological activity even after five days at 37°C. The increase in the stability of FGF2 in cell-culture enables a more homogenous, undifferentiated stem cell culture, while saving scientists crucial time and money, as frequent supplementation of FGF-basic and the everyday medium change is not necessary. Thermostable FGF-2 is a hyperstable protein. The Thermal stability of the protein is increased by 15°C compared to the wild-type FGF-2. Thermostable FGF-2 is more than 5-times prolonged half-life in human cell culture incubated at 37°C. The FGF-2 Thermostable protein is engineered with fully retained biological function and has no harmful stabilizing additives.Thermostable FGF2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 154 amino acids and having a total calculated molecular mass is 17.2kDa.

Source

Escherichia Coli.

Formulation

FGF Basic Thermostable was lyophilized from 20mM Tris-HCl, 150mM NaCl & 5% Trehalose, pH-7.6.

Purity

Purity is greater than 95% as determined by SDS-PAGE.

Biological Activity

The ED50 as calculated by the dose-dependent proliferation of murine balb/c 3T3 cells is less than 0.05ng/ml, corresponding to a specific activity of >20,000,000 units/mg

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Synonyms
FGF2 Thermostable, FGF-basic Thermostable.
Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Thermostable FGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FGF2 Thermostable should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized FGF2 thermostable protein in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AAGSITTLPA LPEDGGSGAF PPGHFKDPKL LYCKNGGFFL RIHPDGRVDG TRDKSDPFIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL YAIKNVTDEC FFFERLEENN YNTYRSRKYP SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS
Background
Why Choose FGF2 Thermostable?
FGF2 can lose much of its activity after 1-2 days at 37°C due to unfolding and degradation. Thermostable FGF2 is engineered with amino acid substitutions that increase structural stability without significantly altering receptor binding or biological function.
What are the advantages of FGF2 Protein?
*Better maintenance of pluripotency markers
*Higher colony quality
*Faster expansion rates
*Reduced spontaneous differentiation
*Greater viability after passaging
What is the source or expression system of FGF2 Protein?
Escherichia Coli.

What is the Purity of FGF2 Protein?
FGF2 Protein is >95% pure as determined by SDS-PAGE.

What is the molecular weight / Mw of FGF2 Protein?
FGF2 Protein having a total Mw of 17.2kDa.

What is the Biological Activity of FGF2 Protein?
The ED50 as calculated by the dose-dependent proliferation of murine balb/c 3T3 cells is less than 0.05ng/ml, corresponding to a specific activity of >20,000,000 units/mg.

What is the endotoxin level for FGF2 Protein?
The endotoxin level is minimal, FGF2 Protein was purified using conventional chromatography techniques.

What is the amino acid sequence of FGF2 Protein?
AAGSITTLPA LPEDGGSGAF PPGHFKDPKL LYCKNGGFFL RIHPDGRVDG TRDKSDPFIK LQLQAEERGV VSIKGVCANR YLAMKEDGRL YAIKNVTDEC FFFERLEENN YNTYRSRKYP SWYVALKRTG QYKLGSKTGP GQKAILFLPM SAKS

Is FGF2 Protein conjugated to a Tag?
FGF2 Protein is not conjugated to a tag.

What applications can FGF2 Protein be used in?
FGF2 Protein can probably be used in western blot, ELISA and Lateral Flow.

ProSpec'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.

Description:

Four And A Half LIM Domains 2 Human Recombinant

AAG11, DRAL, FHL-2, SLIM-3, SLIM3, Four and a half LIM domains protein 2, LIM domain protein DRAL, Skeletal muscle LIM-protein 3, FHL2, RNA Binding Motif Protein 18, RNA-Binding Motif Protein 18, RBM18.

Product # :

PRO-2110

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Description

FHL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-279 a.a) and having a molecular mass of 34.6kDa. FHL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

FHL2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Four And A Half LIM Domains 2 (FHL2) belongs to the four-and-a-half-LIM-only protein family. Family members are comprised of 2 highly conserved, tandemly arranged, zinc finger domains with 4 highly conserved cysteines binding a zinc atom in each zinc finger. The FHL2 protein is assumed to play a part in the assembly of extracellular membranes. Furthermore, FHL2 is down-regulated during transformation of normal myoblasts to rhabdomyosarcoma cells and the FHL2 functions as a link between presenilin-2 and an intracellular signaling pathway.
Synonyms
AAG11, DRAL, FHL-2, SLIM-3, SLIM3, Four and a half LIM domains protein 2, LIM domain protein DRAL, Skeletal muscle LIM-protein 3, FHL2, RNA Binding Motif Protein 18, RNA-Binding Motif Protein 18, RBM18.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMTERFDC HHCNESLFGK KYILREESPY CVVCFETLFA NTCEECGKPI GCDCKDLSYK DRHWHEACFH CSQCRNSLVD KPFAAKEDQL LCTDCYSNEY SSKCQECKKT IMPGTRKMEY KGSSWHETCF ICHRCQQPIG TKSFIPKDNQ NFCVPCYEKQ HAMQCVQCKK PITTGGVTYR EQPWHKECFV CTACRKQLSG QRFTARDDFA YCLNCFCDLY AKKCAGCTNP ISGLGGTKYI SFEERQWHND CFNCKKCSLS LVGRGFLTER DDILCPDCGK DI.

ProSpec'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.

Description:

Cholinergic Receptor Nicotinic, Alpha 6 Human Recombinant

CHNRA6, Neuronal acetylcholine receptor subunit alpha-6, CHRNA6.

Product # :

PRO-1878

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Description

CHRNA6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (26-239 a.a) and having a molecular mass of 29.3kDa. CHRNA6 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CHRNA6 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Cholinergic Receptor Nicotinic, Alpha 6 (CHRNA6) is a part of the nicotinic acetylcholine receptors (nAChRs) family. nAChRs are heteropentameric ligand-gated ion channels generating from the assembly of alpha and beta protein subunits. After binding acetylcholine, the AChRs respond by a major change in conformation which affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. CHRNA6 receptors have a rather selective localization to the nigrostriatal pathway.
Synonyms
CHNRA6, Neuronal acetylcholine receptor subunit alpha-6, CHRNA6.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSKGCV GCATEERLFH KLFSHYNQFI RPVENVSDPV TVHFEVAITQ LANVDEVNQI METNLWLRHI WNDYKLRWDP MEYDGIETLR VPADKIWKPD IVLYNNAVGD FQVEGKTKAL LKYNGMITWT PPAIFKSSCP MDITFFPFDH QNCSLKFGSW TYDKAEIDLL IIGSKVDMND FWENSEWEII DASGYKHDIK YNCCEEIYTD ITYSFYIRRL.

ProSpec'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.

Description:

Zinc Finger Protein 689 Human Recombinant

Zinc Finger Protein 689, Transcription-Involved Protein Upregulated in HCC 1, TIPUH1.

Product # :

PRO-1737

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Description

ZNF689 Human Recombinant produced in E. coli is a single, non-glycosylated polypeptide chain containing 523 amino acids (1-500a.a) and having a molecular mass of 59.3kDa.ZNF689 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

ZNF689 protein solution (1.0mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Zinc Finger Protein 689 (ZNF689) is a member of the krueppel C2H2-type zinc-finger protein family. The ZNF689 protein contains 12 C2H2-type zinc fingers and 1 KRAB domain. ZNF689 may be involved in transcriptional regulation.
Synonyms
Zinc Finger Protein 689, Transcription-Involved Protein Upregulated in HCC 1, TIPUH1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAPPSAP LPAQGPGKAR PSRKRGRRPR ALKFVDVAVY FSPEEWGCLR PAQRALYRDV MRETYGHLGA LGCAGPKPAL ISWLERNTDD WEPAALDPQE YPRGLTVQRK SRTRKKNGEK EVFPPKEAPR KGKRGRRPSK PRLIPRQTSG GPICPDCGCT FPDHQALESH KCAQNLKKPY PCPDCGRRFS YPSLLVSHRR AHSGECPYVC DQCGKRFSQR KNLSQHQVIH TGEKPYHCPD CGRCFRRSRS LANHRTTHTG EKPHQCPSCG RRFAYPSLLA IHQRTHTGEK PYTCLECNRR FRQRTALVIH QRIHTGEKPY PCPDCERRFS SSSRLVSHRR VHSGERPYAC EHCEARFSQR STLLQHQLLH TGEKPYPCPD CGRAFRRSGS LAIHRSTHTE EKLHACDDCG RRFAYPSLLA SHRRVHSGER PYACDLCSKR FAQWSHLAQH QLLHTGEKPF PCLECGRCFR QRWSLAVHKC SPKAPNCSPR SAIGGSSQRG NAH.

ProSpec'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.

Description:

Relaxin-2 Human Recombinant

Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.

Product # :

PRO-1327

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Description

RLN2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 184 amino acids (25-185 a.a) and having a molecular mass of 20.7kDa.RLN2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

RLN2 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Prorelaxin H2 (RLN2) is a member of a family which is produced by the ovary, targets the mammalian reproductive system to ripen the cervix, elongate the pubic symphysis and inhibit uterine contraction. It may also have other roles in boosting sperm motility, regulating blood pressure, controlling heart rate and releasing vasopressin. RLN2 is a peptide hormone linked to several therapeutically relevant physiological effects, including regulation of collagen metabolism and multiple vascular control pathways. The active form of the RLN2 protein consists of an A chain and a B chain linked by disulfide bonds.
Synonyms
Prorelaxin H2, RLN2, H2, RLXH2, H2-RLX, bA12D24.1.1, bA12D24.1.2.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSDSWMEEV IKLCGRELVR AQIAICGMST WSKRSLSQED APQTPRPVAE IVPSFINKDT ETINMMSEFV ANLPQELKLT LSEMQPALPQ LQQHVPVLKD SSLLFEEFKK LIRNRQSEAA DSSPSELKYL GLDTHSRKKR QLYSALANKC CHVGCTKRSL ARFC.

ProSpec'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.

Description:

Ribosomal Protein L18A Human Recombinant

Ribosomal Protein L18a, Ribosomal Protein L18a-Like Protein, 60S Ribosomal Protein L18a, L18A, RPL18A.

Product # :

PRO-1958

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Description

RPL18A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (1-176) and having a molecular mass of 23.2 kDa.RPL18A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The RPL18A solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Ribosomal Protein L18A (RPL18A) is a ribosomal protein which is a component of the 60S subunit, belongs to the L18AE family of ribosomal proteins. RPL18A is located in the cytoplasm. RPL18A is co-transcribed with the U68 snoRNA, which is located in its 3rd intron. The RPL18A protein may play a role in viral replication by interacting with the hepatitis C virus internal ribosome entry site (IRES).
Synonyms
Ribosomal Protein L18a, Ribosomal Protein L18a-Like Protein, 60S Ribosomal Protein L18a, L18A, RPL18A.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMKASGTL REYKVVGRCL PTPKCHTPPL YRMRIFAPNH VVAKSRFWYF VSQLKKMKKS SGEIVYCGQV FEKSPLRVKN FGIWLRYDSR SGTHNMYREY RDLTTAGAVT QCYRDMGARH RARAHSIQIM KVEEIAASKC RRPAVKQFHD SKIKFPLPHR VLRRQHKPRF TTKRPNTFF.

ProSpec'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.

Description:

Connective Tissue Growth Factor Human Recombinant, His Tag

CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.

Product # :

CYT-438

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Description

CTGF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (27-349) and having a molecular mass of 37.7kDa.The CTGF is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

CTGF protein (1mg/ml) is supplied in 20mM Tris-HCl, pH-8 and 10% Glycerol.

Purity

Greater than 85.0% as determined by Analysis by SDS-PAGE.

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Introduction
Connective Tissue Growth Factor belongs to the CCN family of proteins. The CCN family presently consists of six members in human also known as: Cyr61 (Cystein rich 61), CTGF (Connective Tissue Growth Factor), Nov (Nephroblastoma Overexpressed gene), WISP-1, 2 and 3 (Wnt-1 Induced Secreted Proteins). The CCN genes encode secreted proteins associated with the Extracellular Matrix (ECM) and cell membrane. CCN proteins are matricellular proteins which are involved in the regulation of various cellular functions including: proliferation, differentiation, survival, adhesion and migration. They are expressed in derivatives of the three embryonic sheets and are implicated in the development of kidney, nervous system, muscle, bone marrow, cartilage and bone. During adulthood, they are implicated in wound healing, bone fracture repair, and pathologies such as: fibrosis, vascular ailments and tumorigenesis.
Full length secreted CCN proteins can show an antiproliferative activity, whereas truncated isoforms are likely to stimulate proliferation and behave as oncogenes. The full length protein consists of four modulesModule I shares partial identity with the N-terminal part of the Insulin-like Growth Factor Binding Proteins (IGFBPs).
Module II includes a stretch of 70amino acid residues – which shares sequence identity with the Von Willebrand Factor Type C repeat (VWC).
Module III contains sequences sharing identity with the Thrombospondin type 1 repeat (TSP1) (WSXCSXXCG), which is thought to be implicated in the binding of sulfated glycoconjugates and to be important for cell adhesion. Module IV, also designated CT, is encoded by exon5. It is the leasts conserved one of the four domains at the level of nucleotide sequence, but it appears to be critical for several of the biological functions attributed to the CCN proteins. Module IV resembles the CT domain of several extracellular protein including, Von Willebrand's factor and mucins. Sequence similarities to heparin-binding motifs are also found within this domain.
Proteolysis of the secreted full-length CCN proteins that has been reported in the case of CCN2 and CCN3 might result in the production of CCN-derived peptides with high affinity for ligands that full-length CNN proteins bind only poorly. Amino-truncated CCN2 isoforms were biologically active whereas no specific biological activity has been attributed to the truncated CCN3. Although the molecular processes underlying the production of these secreted isoforms is presently unknown, it is important to note that proteolysis occur at the same amino acid residues in both CCN2 and CCN3. An elevated expression of CCN2 has also been detected by Northern blotting in human invasive mammary ductal carcinomas, dermatofibromas, pyogenic granuloma, endothelial cells of angiolipomas and angioleiomyomas, and in pancreatic tumors. A study performed with chondrosarcomas representative of various histological grades established that CCN2 expression was closely correlated with increasing levels of malignancy. In agreement with CCN2 playing a role in brain tumor angiogenesis, immunocytochemistry studies indicated that both glioblastoma tumor cells and proliferating endothelial cells stained positive for CCN2. In astrocytomas, CCN2 expression was particularly elevated in high grade tumors, with a marked effect of CCN2 on cell proliferation. Downregulation of CCN2 expression in these cells was associated with a growth arrest at the G1/S transition while over-expression of CCN2 induced a two-fold increase of the number of cells in the G1 phase. Gene profiling analysis allowed to identify a set of about 50 genes whose expression might account for the proliferative activity of CCN2 in these cells. CCN2 was seen in a higher proportion of mononuclear cells of patients with acute lymphoblastic leukemia.
Synonyms
CCN2, NOV2, HCS24, IGFBP8, MGC102839, CTGF, Connective Tissue Growth Factor.
Physical Appearance
Sterile Filtered clear solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQNCSGPCRC PDEPAPRCPA GVSLVLDGCG CCRVCAKQLG ELCTERDPCD PHKGLFCDFG SPANRKIGVC TAKDGAPCIF GGTVYRSGES FQSSCKYQCT CLDGAVGCMP LCSMDVRLPS PDCPFPRRVK LPGKCCEEWV CDEPKDQTVV GPALAAYRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK CIRTPKISKP IKFELSGCTS MKTYRAKFCG VCTDGRCCTP HRTTTLPVEF KCPDGEVMKK NMMFIKTCAC HYNCPGDNDI FESLYYRKMY GDMA.
Background
What is the molecular weight/Mw of CTGF Protein?
CTGF Protein has a total Mw of 37.7kDa.

What is the source or expression system of CTGF Protein?
Escherichia Coli.

What is the Purity of CTGF Protein?
CTGF Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of CTGF Protein?
The biological functionality of CTGF Protein will be determined in the future.

What is the amino acid sequence of CTGF Protein?
MGSSHHHHHH SSGLVPRGSH MQNCSGPCRC PDEPAPRCPA GVSLVLDGCG CCRVCAKQLG ELCTERDPCD PHKGLFCDFG SPANRKIGVC TAKDGAPCIF GGTVYRSGES FQSSCKYQCT CLDGAVGCMP LCSMDVRLPS PDCPFPRRVK LPGKCCEEWV CDEPKDQTVV GPALAAYRLE DTFGPDPTMI RANCLVQTTE WSACSKTCGM GISTRVTNDN ASCRLEKQSR LCMVRPCEAD LEENIKKGKK CIRTPKISKP IKFELSGCTS MKTYRAKFCG VCTDGRCCTP HRTTTLPVEF KCPDGEVMKK NMMFIKTCAC HYNCPGDNDI FESLYYRKMY GDMA.

What applications can CTGF Protein be used in?
CTGF Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CTGF Protein?
The endotoxin level is minimal, CTGF Protein was purified using conventional chromatography techniques.

ProSpec'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.

Description:

Heat Shock Factor Binding Protein - 1 Human Recombinant

NPC-A-13, HSBP1, Heat shock factor-binding protein 1, Nasopharyngeal carcinoma-associated antigen 13, HSF1BP, DKFZp686D1664, DKFZp686O24200.

Product # :

HSP-001

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Description

Recombinant Human HSBP1 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 76 amino acids and having a molecular mass of 8.5 kDa.

Source

Escherichia Coli.

Formulation

The HSBP1 protein (1mg/ml) solution contains 20mM Tris-HCl buffer pH-7.5, 50mM NaCl, 1mM EDTA and 20% Glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
The heat-shock response is elicited by exposure of cells to thermal and chemical stress and through the activation of HSFs (heat shock factors) results in the elevated expression of heat-shock induced genes. Heat shock factor binding protein-1 (HSBP1), is a 76-amino-acid protein that binds to heat shock factor 1(HSF1), which is a transcription factor involved in the HS response. During HS response, HSF1 undergoes conformational transition from an inert non-DNA-binding monomer to active functional trimers. HSBP1 is nuclear-localized and interacts with the active trimeric state of HSF1 to negatively regulate HSF1 DNA-binding activity. Overexpression of HSBP1 in mammalian cells represses the transactivation activity of HSF1. When overexpressed in C.elegans HSBP1 has severe effects on survival of the animals after thermal and chemical stress consistent with a role of HSBP1 as a negative regulator of heat shock response.
Synonyms
NPC-A-13, HSBP1, Heat shock factor-binding protein 1, Nasopharyngeal carcinoma-associated antigen 13, HSF1BP, DKFZp686D1664, DKFZp686O24200.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MAETDPKTVQ DLTSVVQTLL QQMQDKFQTM SDQIIGRIDD MSSRIDDLEK NIADLMTQAG VEELESENKI PATQKS.

ProSpec'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.

Description:

Heat shock 70kDa protein 5 Human Recombinant, Hi-5

78 kDa glucose-regulated protein, GRP-78, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein, BiP, HSPA5, GRP78, MIF2, FLJ26106.

Product # :

HSP-037

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Description

HSPA5 produced in Hi-5 cells is a single, glycosylated polypeptide chain containing 640 amino acids (20-650 a.a.) and having a molecular mass of 71kDa. HSPA5 is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Hi-5 Cells.

Formulation

The HSPA5 protein solution (1mg/ml) 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 200mM NaCl.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Binding immunoglobulin protein (BiP or HSPA5) is a member of the family of ~70kDa heat shock proteins (HSP 70). HSPA5 is a stress response protein which is induced by agents or conditions that adversely affect endoplasmic reticulum (ER) function. HSPA5 is crucial for the proper glycosylation, folding as well as for the maintenance of cell homeostasis and the prevention of apoptosis.
Synonyms
78 kDa glucose-regulated protein, GRP-78, Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78, Heat shock 70 kDa protein 5, Immunoglobulin heavy chain-binding protein, BiP, HSPA5, GRP78, MIF2, FLJ26106.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MEEDKKEDVG TVVGIDLGTT YSCVGVFKNG RVEIIANDQG NRITPSYVAF TPEGERLIGD AAKNQLTSNP ENTVFDAKRL IGRTWNDPSV QQDIKFLPFK VVEKKTKPYI QVDIGGGQTK TFAPEEISAM VLTKMKETAE AYLGKKVTHA VVTVPAYFND AQRQATKDAG TIAGLNVMRI INEPTAAAIA YGLDKREGEK NILVFDLGGG TFDVSLLTID NGVFEVVATN GDTHLGGEDF DQRVMEHFIK LYKKKTGKDV RKDNRAVQKL RREVEKAKRA LSSQHQARIE IESFYEGEDF SETLTRAKFE ELNMDLFRST MKPVQKVLED SDLKKSDIDE IVLVGGSTRI PKIQQLVKEF FNGKEPSRGI NPDEAVAYGA AVQAGVLSGD QDTGDLVLLD VCPLTLGIET VGGVMTKLIP RNTVVPTKKS QIFSTASDNQ PTVTIKVYEG ERPLTKDNHL LGTFDLTGIP PAPRGVPQIE VTFEIDVNGI LRVTAEDKGT GNKNKITITN DQNRLTPEEI ERMVNDAEKF AEEDKKLKER IDTRNELESY AYSLKNQIGD KEKLGGKLSS EDKETMEKAV EEKIEWLESH QDADIEDFKA KKKELEEIVQ PIISKLYGSA GPPPTGEEDT AELEHHHHHH.

ProSpec'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.

Description:

Granulocyte-Colony Stimulating Factor Human Recombinant

CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Lenograstim, G-CSF, MGC45931, GCSF.

Product # :

CYT-220

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Description

Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8 KD.GCSF is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

GCSF was lyophilized after extensive dialysis against 10mM sodium acetate buffer pH= 4.

Purity

Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml, corresponding to a Specific Activity of 100,000,000 IU/mg.

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Introduction
GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Lenograstim, G-CSF, MGC45931, GCSF.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GCSF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GCSF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized GCSF in sterile 20mM AcOH not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids of GCSF was determined and was found to be Met-Thr-Pro-Leu-Gly.
Background
What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein has a total Mw of 18.8kDa.

What is the source or expression system of GDF15 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein is >98% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF15 HUMAN, HIS Protein?
The ED50, calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml, corresponding to a Specific Activity of 100,000,000 IU/mg.

What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein is composed from 175 amino acids.

What applications can GDF15 HUMAN, HIS Protein be used in?
GDF15 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GDF15 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF15 HUMAN, HIS Protein was purified using conventional chromatography techniques.
Protein content
GCSF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.815 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of GCSF as a Reference Standard.

ProSpec'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.

Description:

Hepatitis A Virus Cellular Receptor 2 Human Recombinant

Hepatitis A virus cellular receptor 2, HAVcr-2, T-cell immunoglobulin and mucin domain-containing protein 3, TIMD-3, T-cell membrane protein 3, TIM-3, HAVCR2, TIM3, TIMD3, TIM3, KIM-3.

Product # :

HAV-224

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Description

Recombinant Human HAVCR2 produced in E. coli is a single polypeptide chain containing 206 amino acids (aa 22-202) and having a molecular mass of 22.7kDa.HAVCR2 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The HAVCR2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

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Introduction
Hepatitis A Virus Cellular Receptor 2 (HAVCR2) is a member of the immunoglobulin superfamily. HACVR2 controls macrophage activation. HACVR2 inhibits T-helper type 1 lymphocyte (Th1)-mediated auto- and alloimmune responses and stimulates immunological tolerance.
Synonyms
Hepatitis A virus cellular receptor 2, HAVcr-2, T-cell immunoglobulin and mucin domain-containing protein 3, TIMD-3, T-cell membrane protein 3, TIM-3, HAVCR2, TIM3, TIMD3, TIM3, KIM-3.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSEVEY RAEVGQNAYL PCFYTPAAPG NLVPVCWGKG ACPVFECGNV VLRTDERDVN YWTSRYWLNG DFRKGDVSLT IENVTLADSG IYCCRIQIPG IMNDEKFNLK LVIKPAKVTP APTLQRDFTA AFPRMLTTRG HGPAETQTLG SLPDINLTQI STLANELRDS RLANDLRDSG ATIRIG.

ProSpec'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.

Description:

Holo Transferrin Human Recombinant

Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.

Product # :

PRO-2844

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Description

Human Holo Transferrin Recombinant produced in HEK Cells is a glycosylated polypeptide containing 679 amino acids and having a Mw of of 76 kDa.

Source

HEK Cells

Formulation

The protein was lyophilized from 1x PBS pH-7.4.

Purity

Protein is >98% pure as determined by 10% PAGE (coomassie staining).

Biological Activity

The activity of Recombinant Holo Transferrin was determined by the proliferation assay using MDCK cells stimulated with recombinant human Holo Transferrin. The protein was found biologically active

sds-page, activity

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Introduction
Recombinant Human Holo Transferrin is an iron-delivery signaling protein which functions in the delivery of Fe³⁺ iron to cells using transferrin receptor-1 (TfR1/CD71).
Holo-transferrin binds TfR1, undergoes receptor-mediated endocytosis and the iron is released intracellularly. Transferrin Human Recombinant is crucial for brain and the nervous system, neuronal mitochondrial metabolism, neurotransmitter synthesis, oligodendrocyte myelination and synaptic activity. Recombinant holo-transferrin can be used in cell therapy, stem-cell expansion, CHO production, or drug-delivery platforms.
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Physical Appearance
Sterile Filtered lyophilized (freeze-dried) powder.
Stability
Store the lyophilized Holo Transferrin recombinant between 2-8°C, do not freeze.
Upon reconstitution Holo Transferrin should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized Holo Transferrin recombinant in sterile 18MΩ-cm H2O at 1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
VPDKTVRWCA VSEHEATKCQ SFRDHMKSVI PSDGPSVACV KKASYLDCIR AIAANEADAV TLDAGLVYDA YLAPNNLKPV VAEFYGSKED PQTFYYAVAV VKKDSGFQMN QLRGKKSCHT GLGRSAGWNI PIGLLYCDLP EPRKPLEKAV ANFFSGSCAP CADGTDFPQL CQLCPGCGCS TLNQYFGYSG AFKCLKDGAG DVAFVKHSTI FENLANKADR DQYELLCLDN TRKPVDEYKD CHLAQVPSHT VVARSMGGKE DLIWELLNQA QEHFGKDKSK EFQLFSSPHG KDLLFKDSAH GFLKVPPRMD AKMYLGYEYV TAIRNLREGT CPEAPTDECK PVKWCALSHH ERLKCDEWSV NSVGKIECVS AETTEDCIAK IMNGEADAMS LDGGFVYIAG KCGLVPVLAE NYNKSDNCED TPEAGYFAVA VVKKSASDLT WDNLKGKKSC HTAVGRTAGW NIPMGLLYNK INHCRFDEFF SEGCAPGSKK DSSLCKLCMG SGLNLCEPNN KEGYYGYTGA FRCLVEKGDV AFVKHQTVPQ NTGGKNPDPW AKNLNEKDYE LLCLDGTRKP VEEYANCHLA RAPNHAVVTR KDKEACVHKI LRQQQHLFGS NVTDCSGNFC LFRSETKDLL FRDDTVCLAK LHDRNTYEKY LGEEYVKAVG NLRKCSTSSL LEACTFRRP.

ProSpec'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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