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1000 results found for “Regulator of Calcineurin”

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  • View Data Sheet

    Description:

    Zinc Finger, CCHC Domain Containing 12 Human Recombinant

    PNMA7A, SIZN, SIZN1, Zinc finger CCHC domain-containing protein 12, Smad-interacting zinc finger protein 1, ZCCHC12.

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    PRO-1982

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    Description

    ZCCHC12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 425 amino acids (1-402 a.a) and having a molecular mass of 47.8kDa. ZCCHC12 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ZCCHC12 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

      Zinc Finger, CCHC Domain Containing 12 (ZCCHC12) which holds 1 CCHC-type zinc finger is a part of the ZCCHC12 family. ZCCHC12 takes part in the bone morphogenetic protein (BMP)-signaling pathway as a transcriptional coactivator. BMP signaling is positively modulated as a result of the interaction between ZCCHC12 with SMAD1 and the association with CBP in the transcription complex.

    • Synonyms

      PNMA7A, SIZN, SIZN1, Zinc finger CCHC domain-containing protein 12, Smad-interacting zinc finger protein 1, ZCCHC12.

    • 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 MGSMASIIAR VGNSRRLNAP LPPWAHSMLR SLGRSLGPIM ASMADRNMKL FSGRVVPAQG EETFENWLTQ VNGVLPDWNM SEEEKLKRLM KTLRGPAREV MRVLQATNPN LSVADFLRAM KLVFGESESS VTAHGKFFNT LQAQGEKASL YVIRLEVQLQ NAIQAGIIAE KDANRTRLQQ LLLGGELSRD LRLRLKDFLR MYANEQERLP NFLELIRMVR EEEDWDDAFI KRKRPKRSES MVERAVSPVA FQGSPPIVIG SADCNVIEID DTLDDSDEDV ILVESQDPPL PSWGAPPLRD RARPQDEVLV IDSPHNSRAQ FPSTSGGSGY KNNGPGEMRR ARKRKHTIRC SYCGEEGHSK ETCDNESDKA QVFENLIITL QELTHTEMER SRVAPGEYND FSEPL.

    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.

    Zcchc12 Human
  • View Data Sheet

    Description:

    Relaxin-2 Human Recombinant

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

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    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.

    Rln2 Human
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    Description:

    Thymus and Activation Regulated Chemokine Human Recombinant (CCL17), His Tag

    C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.

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    CHM-359

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    Description

    TARC Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 92 amino acids (24-94 a.a.) and having a molecular mass of 10.3 kDa. The TARC is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TARC protein contains 1xPBS (pH7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      TARC cDNA encodes a 94 amino acid precursor protein with a 23 amino acid residue signal peptide that is cleaved off to generate the 71 amino acid residue mature secreted protein. Along with CC chemokine family members, CCL-17 has approximately 24-29% amino acid sequence identity with RANTES, MIP-1a, MIP-1b, MCP-1, MCP-2, MCP-3 and I-309. TARC is expressed in thymus, and at a lower level in the lung, colon, and small intestine. TARC is in addition transiently expressed in stimulated peripheral blood mononuclear cells. Recombinant TARC has been shown to be chemotactic for T cell lines but not monocytes or neutrophils. CCL-17 was recently identified to be a specific functional ligand for CCR4, a receptor that is selectively expressed on T cells. CCL17 is one of quite a few Cys-Cys (CC) cytokine genes clustered on the q arm of chromosome 16. CCL17 shows chemotactic activity for T lymphocytes, but not monocytes or granulocytes. CCL17 binds to chemokine receptors CCR4 and CCR8. This chemokine plays important roles in T cell development in thymus as well as in trafficking and activation of mature T cells.

    • Synonyms

      C-C motif chemokine 17, Small-inducible cytokine A17, Thymus and activation-regulated chemokine, CC chemokine TARC, ABCD-2, CCL17, CCL-17, SCYA17, TARC, A-152E5.3, MGC138271, MGC138273.

    • 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 MARGTNVGRE CCLEYFKGAI PLRKLKTWYQ TSEDCSRDAI VFVTVQGRAI CSDPNNKRVK NAVKYLQSLE RS.

    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.

    Tarc Human His
  • View Data Sheet

    Description:

    Crystallin, Mu Human Recombinant

    Crystallin Mu, Thiomorpholine-Carboxylate Dehydrogenase, THBP, NADP-Regulated Thyroid-Hormone Binding Protein, NADP-Regulated Thyroid-Hormone-Binding Protein, Mu-Crystallin Homolog, EC 1.5.1.25, DFNA40, CRYM.

    Product # :

    PRO-2291

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    Description

    CRYM Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 334 amino acids (1-314) and having a molecular mass of 35.9kDa. CRYM is fused to 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CYRM 1mg/ml solution containing 20mM Tris-HCl buffer (pH8.0), 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Crystallin, Mu (CRYM) is a taxon-specific crystallin protein which binds NADPH and has sequence similarity to bacterial ornithine cyclodeaminases. CRYM doesn’t perform a structural role in lens tissue; instead CRYM binds thyroid hormone for possible regulatory or developmental roles. CRYM gene mutations are linked with autosomal dominant non-syndromic deafness. CRYM specifically catalyzes the reduction of imine bonds in brain substrates which may include cystathionine ketamine and lanthionine ketamine.

    • Synonyms

      Crystallin Mu, Thiomorpholine-Carboxylate Dehydrogenase, THBP, NADP-Regulated Thyroid-Hormone Binding Protein, NADP-Regulated Thyroid-Hormone-Binding Protein, Mu-Crystallin Homolog, EC 1.5.1.25, DFNA40, CRYM.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      CRYM although stable at 4°C for 1 week, should be stored 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSRVPAFLSA AEVEEHLRSS SLLIPPLETA LANFSSGPEG GVMQPVRTVV PVTKHRGYLG VMPAYSAAED ALTTKLVTFY EDRGITSVVP SHQATVLLFE PSNGTLLAVM DGNVITAKRT AAVSAIATKF LKPPSSEVLC ILGAGVQAYS HYEIFTEQFS FKEVRIWNRT KENAEKFADT VQGEVRVCSS VQEAVAGADV IITVTLATEP ILFGEWVKPG AHINAVGASR PDWRELDDEL MKEAVLYVDS QEAALKESGD VLLSGAEIFA ELGEVIKGVK PAHCEKTTVF KSLGMAVEDT VAAKLIYDSW SSGK

    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.

    Crym Human
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    Description:

    VEGF Co-regulated Chemokine 1 Human Recombinant

    VEGF coregulated chemokine 1, C-X-C motif chemokine 17, Dendritic cell and monocyte chemokine-like protein, DMC, CXCL17, VCC1, Dcip1, VCC-1, UNQ473.

    Product # :

    CHM-019

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    Description

    CXCL17 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 98 amino acids and having a molecular mass of 11.5kDa.The CXCL17 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CXCL17 protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4, containing 3% Trehalose.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by its ability to induce VEGF expression using murine endothelial cells is less than 5.0µg/ml, corresponding to a specific activity of > 200IU/mg.

    More Info

    • Introduction

      Dendritic cell and monocyte chemokinelike protein (DMC/CXCL17/VEGF-correlated chemokine 1/VCC1), is a secreted molecule with a size and predicted 3-dimensional folding pattern similar to that of chemokines CXCL8/IL8 and CXCL14/BRAK. CXCL17 is constitutively generated by airway and intestinal epithelium. CXCL17 induces the chemotaxis of quiescent, but not LPS-activated peripheral blood monocytes and dendritic cells, and it also binds these cells specifically. The expression of CXCL17 is increased in endothelial cells when they are induced to form tubes in vitro. CXCL17, CXCL1/GRO and CXCL8/IL8 which have roles in angiogenesis, show significantly correlated expression with that of VEGF in primary lung, breast and esophageal tumors. Therefore, CXCL17 is suggested to have a role in tumor angiogenesis. The mature Rat CXCL17 shares 82%, 71% amino acid sequence identity with mouse, human CXCL17, respectively.

    • Synonyms

      VEGF coregulated chemokine 1, C-X-C motif chemokine 17, Dendritic cell and monocyte chemokine-like protein, DMC, CXCL17, VCC1, Dcip1, VCC-1, UNQ473.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL17 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL17 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 CXCL17 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SSLNPGVARG HRDRGQASRR WLQEGGQECE CKDWFLRAPR RKFMTVSGLP KKQCPCDHFK GNVKKTRHQR HHRKPNKHSR ACQQFLKQCQ LRSFALPL.

    • Background

      What is the molecular weight/Mw of CXCL17 HUMAN Protein?
      CXCL17 HUMAN Protein has a total Mw of 11.5kDa.

      What is the source or expression system of CXCL17 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CXCL17 HUMAN Protein?
      CXCL17 HUMAN Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL17 HUMAN Protein?
      The ED50 as determined by its ability to induce VEGF expression using murine endothelial cells is less than 5.0µg/ml, corresponding to a specific activity of > 200IU/mg.

      What is the amino acid sequence of CXCL17 HUMAN Protein?
      SSLNPGVARG HRDRGQASRR WLQEGGQECE CKDWFLRAPR RKFMTVSGLP KKQCPCDHFK GNVKKTRHQR HHRKPNKHSR ACQQFLKQCQ LRSFALPL.

      What applications can CXCL17 HUMAN Protein be used in?
      CXCL17 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL17 HUMAN Protein?
      The endotoxin level is minimal, CXCL17 HUMAN 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.

    Cxcl17 Human
  • View Data Sheet

    Description:

    Renin Human Recombinant, sf9

    REN, HNFJ2, Renin, Angiotensinogenase.

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    PRO-2342

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    Description

    REN Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 391 amino acids (24-406) and having a molecular mass of 43.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).REN is fused to 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    REN protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      Renin is a highly specific endopeptidase which generates angiotensin I from angiotensinogen in the plasma. angiotensin I is an important regulator of blood pressure and electrolyte balance. Renin initiates a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.

    • Synonyms

      REN, HNFJ2, Renin, Angiotensinogenase.

    • 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

      LPTDTTTFKR IFLKRMPSIR ESLKERGVDM ARLGPEWSQP MKRLTLGNTT SSVILTNYMD TQYYGEIGIG TPPQTFKVVF DTGSSNVWVP SSKCSRLYTA CVYHKLFDAS DSSSYKHNGT ELTLRYSTGT VSGFLSQDII TVGGITVTQM FGEVTEMPAL PFMLAEFDGV VGMGFIEQAI GRVTPIFDNI ISQGVLKEDV FSFYYNRDSE NSQSLGGQIV LGGSDPQHYE GNFHYINLIK TGVWQIQMKG VSVGSSTLLC EDGCLALVDT GASYISGSTS SIEKLMEALG AKKRLFDYVV KCNEGPTLPD ISFHLGGKEY TLTSADYVFQ ESYSSKKLCT LAIHAMDIPP PTGPTWALGA TFIRKFYTEF DRRNNRIGFA LARLEHHHHH H.

    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.

    Ren Human Sf9
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    Description:

    Osteoprotegerin Human Recombinant, His Tag

    TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.

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    CYT-290

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    Description

    Recombinant Human OCIF produced in E.coli cells is a single, non-glycosylated, polypeptide chain containing amino acids 201-401 and having a molecular mass of 31 kDa which includes a 4 kDa His tag.The OPG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 1X PBS, 0.1% SDS and 1mM DTT.

    Purity

    Greater than 80.0% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

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    • Introduction

      Osteoprotegerin, which is a member of the tumor necrosis factor receptor superfamily and is involved in the regulation of bone metabolism. OPGand its ligand (OPGL) are cytokines regulating osteoclasto-genesis. OPGL binds to receptors on the surface of preosteoclasts and stimulates their differentiation into active osteoclasts. This leads to osteoresorption. OPG inhibits this osteoclasto-genesis (OPG is secreted by osteoblasts, and binds to OPGL, thus inhibiting maturation of osteoclasts and osteoresorption). The degree and activity of osteoresorption depend mainly on the balance between OPG and its ligand (OPGL); factors increasing OPGL expression mostly reduce OPG expression and vice versa.

    • Synonyms

      TNFRSF11B, OPG, OCIF, Osteoclastogenesis inhibitory factor, TR1, MGC29565.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Osteoprotegerin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution OCIF 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 Osteoprotegerin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Applications

      1. Positive control for Western blot.
      2. Antibody production.
      3. Protein assay.

    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.

    Osteoprotegerin Human His
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    Description:

    GRO-Beta Mouse Recombinant (CXCL2)

    Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.

    Product # :

    CHM-338

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    Description

    GRO-Beta Mouse Recombinant also caled mouse MIP-2 produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7849 Dalton. The CXCL2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 150mM NaCl.

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The Biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 105-106units/mg.

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    • Introduction

      Chemokine (C-X-C motif) ligand 2 (CXCL2) is a small cytokine belonging to the CXC chemokine family that is also called macrophage inflammatory protein 2-alpha (MIP2-alpha), Growth-regulated protein beta (Gro-beta) and Gro oncogene-2 (Gro-2). CXCL2 is 90% identical in amino acid sequence as a related chemokine, CXCL1. This chemokine is secreted by monocytes and macrophages and is chemotactic for polymorphonuclear leukocytes and hematopoietic stem cells. The gene for CXCL2 is located on human chromosome 4 in a cluster of other CXC chemokines. CXCL2 mobilizes cells by interacting with a cell surface chemokine receptor called CXCR2.

    • Synonyms

      Macrophage inflammatory protein 2-alpha, MIP2-alpha, CXCL2, Growth- regulated protein beta, Gro-beta, chemokine (C-X-C motif) ligand 2, GRO2, GROb, MIP2, MIP2A, SCYB2, MGSA-b, MIP-2a, CINC-2a, MGSA beta.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL2 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 GRO-beta Mouse in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AVVASELRCQ CLKTLPRVDF KNIQSLSVTP PGPHCAQTEV IATLKGGQKV CLDPEAPLVQ KIIQKILNKG KAN.

    • Background

      What is the molecular weight/Mw of CXCL2 MOUSE Protein?
      CXCL2 MOUSE Protein has a total Mw of 7.84kDa.

      What is the source or expression system of CXCL2 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of CXCL2 MOUSE Protein?
      CXCL2 MOUSE Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL2 MOUSE Protein?
      The Biological activity was determined by its ability to chemoattract total human neutrophils using a concentration range of 1.0-10.0 ng/ml, corresponding to a specific activity of 105-106units/mg.

      What is the amino acid sequence of CXCL2 MOUSE Protein?
      AVVASELRCQ CLKTLPRVDF KNIQSLSVTP PGPHCAQTEV IATLKGGQKV CLDPEAPLVQ KIIQKILNKG KAN.

      What applications can CXCL2 MOUSE Protein be used in?
      CXCL2 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL2 MOUSE Protein?
      The endotoxin level is minimal, CXCL2 MOUSE Protein was purified using conventional chromatography techniques.


    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.015 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 standard solution of GRO-b as a Reference Standard.

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    Gro Beta Mouse
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    Description:

    Activin-A Human Recombinant, Active

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-145

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    Description

    Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

    Source

    E.Coli.

    Formulation

    Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.

    Purity

    Greater than 95% as obsereved by SDS-PAGE.

    Biological Activity

    Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 105 units/mg.

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

      Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A 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

      Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.

    • Background

      Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential

      Introduction:

      Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.

      Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.

      Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.

      Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.

      The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.

      In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.

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    Inhba Human
  • View Data Sheet

    Description:

    Activin-B Human Recombinant, Active

    Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

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    CYT-057

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    Description

    Activin B human Recombinant produced in Nicotiana benthamiana plant is a beta-B single chain (aa 293-406) containing 123 amino acids (molecular formula C615H910N178O177S12). Activin B is fused to a 10-His-tag at the N-terminal having the total molecular mass of 14kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 0.05M Tris-HCl buffer pH 7.4.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

    More Info

    • Synonyms

      Inhibin beta B (activin AB beta polypeptide), Inhibin, beta-2, Activin beta-B chain, MGC157939.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Activin B although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin B 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 Activin B in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG.

    • Background

      An Investigation into the Functional Roles and Therapeutic Potential of Activin-B Human Recombinant, Active

      1. Abstract

      Activin-B Human Recombinant, Active, also referred to as beta-2, Activin beta-B chain, or MGC157939, is a crucial component of the Transforming Growth Factor-beta (TGF-beta) superfamily. The multifaceted nature of this protein implicates it in numerous physiological processes. This paper delves into the bioactivity of Activin-B, exploring its role in cellular proliferation, differentiation, apoptosis, and its potential for therapeutic applications, especially in the realms of regenerative medicine, reproductive health, and cancer therapy.

      2. Introduction

      The TGF-beta superfamily, of which Activin-B is a member, is renowned for its far-reaching implications in cell and developmental biology. This superfamily boasts members that control cell growth, differentiation, and apoptosis, thus playing vital roles in organogenesis, bone growth, and reproductive functions. This research paper aims to shed light on the characteristics and potential therapeutic applications of Activin-B.

      3. Structure and Synthesis of Activin-B

      Activin-B is a dimeric protein, composed of two identical beta-B chains. This homodimer undergoes multiple stages of synthesis, starting as a precursor protein, which then experiences proteolytic processing to eventually form the mature peptide. It is this coordinated activity of various enzymes and molecular chaperones that ensure the accurate biosynthesis of Activin-B.

      4. Biological Functions of Activin-B

      Activin-B's roles extend from embryogenesis and organogenesis to the modulation of reproductive functions. Its influence over cellular proliferation, differentiation, and apoptosis has significant repercussions in physiological and pathological scenarios. Its regulatory functions also encompass immunomodulation and wound healing, underpinning its extensive biological reach.

      5. Activin-B in Regenerative Medicine

      Regenerative medicine's primary focus is the repair and regeneration of tissues, and it is here that the potential of Activin-B shines. The protein's capacity to regulate cellular processes positions it as a possible agent in tissue repair, making it an intriguing research topic for therapeutic applications in regenerative medicine.

      6. Activin-B and Reproductive Health

      Activin-B’s role in reproductive health is undeniable, having been implicated in follicular development, ovulation, and pregnancy maintenance. Its potent influence on reproductive functions indicates the possibility of its use in the treatment of reproductive disorders, providing a potential pathway for further therapeutic development.

      7. Activin-B in Cancer

      Recent research has connected the deregulation of Activin-B to various types of cancer. Deciphering the mechanisms through which Activin-B affects cancer cell proliferation and survival could open up new avenues for targeted cancer therapy. This critical linkage emphasizes the need for comprehensive studies on Activin-B's role in oncogenesis.

      8. Conclusion and Future Perspectives

      Our understanding of Activin-B's biological functions has grown immensely, but many mysteries remain. The continued exploration of the molecular mechanisms through which Activin-B operates will undoubtedly yield more insights into its potential therapeutic uses, guiding the development of new treatments for a myriad of diseases.

      What is the molecular weight / Mw of Activin B Protein?
      Activin A Protein has a total Mw of 14 kDa.

      What is the source or expression system of Activin B Protein?
      Nicotinia

      What is the Purity of Activin B Protein?
      Activin B Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of Activin B Protein?
      The biological activity of Activin B is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation. EC50 <5ng/ml is required to stimulate a half-maximal response at cytokine saturation. Note: Since applications vary, each investigator should titrate the reagent to obtain optimal results.

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

      What is the amino acid sequence of ACTIVIN B Protein?
      HHHHHHHHHH GLECDGRTNL CCRQQFFIDF RLIGWNDWII APTGYYGNYC EGSCPAYLAG VPGSASSFHT AVVNQYRMRG LNPGTVNSCC IPTKLSTMSM LYFDDEYNIV KRDVPNMIVE ECG

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

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    Activin B Human Active
  • View Data Sheet

    Description:

    Betacellulin Human Recombinant, His Tag

    Betacellulin, Probetacellulin. 

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    CYT-077

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    • sds-page

    Description

    BTC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 101 amino acids (32-111) and having a molecular mass of 11.3 kDa.BTC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The BTC solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 0.2M NaCl and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

      Btc is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells. The effects of betacellulin are probably mediated by the egf receptor and other related receptors.

    • Synonyms

      Betacellulin, Probetacellulin.

    • 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 MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y

    • Background

      What is the molecular weight/Mw of BETACELLULIN Protein?
      BETACELLULIN Protein has a total Mw of 11.3kDa.

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

      What is the Purity of BETACELLULIN Protein?
      BETACELLULIN Protein is >90% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of BETACELLULIN Protein?
      MGSSHHHHHH SSGLVPRGSH MDGNSTRSPE TNGLLCGDPE ENCAATTTQS KRKGHFSRCP KQYKHYCIKG RCRFVVAEQT PSCVCDEGYI GARCERVDLF Y

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

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

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    Btc His Human
  • View Data Sheet

    Description:

    Interleukin-1 Receptor Antagonist Mouse Recombinant

    IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, F630041P17Rik.

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    CYT-658

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    Description

    IL1 ra Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 153 amino acids and having a molecular mass of 17.4kDa. The IL1ra is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution in water containing NaHCO3.

    Purity

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

    Biological Activity

    The mouse IL-1Ra is capable of inhibiting IL-1-alpha activity in helper T cell line D10.G4.1.

    More Info

    • Introduction

      Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.

    • Synonyms

      IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, F630041P17Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Interleukin 1ra although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-1ra 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 Interleukin-1ra in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Cys-Arg-Pro-Ser-Gly.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.91 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).

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    Il 1Ra Mouse
  • View Data Sheet

    Description:

    Interleukin-1 Receptor Antagonist Mouse Recombinant, His Tag

    IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, F630041P17Rik.

    Product # :

    CYT-136

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    Description

    IL-1RA mouse Recombinant produced E. coli is a single polypeptide chain containing 177 amino acids (27-178) and having a molecular mass of 20kDa.IL-1RA is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-1 ra is a member of the interleukin 1 cytokine family. This protein inhibits the activities of interleukin 1, alpha (IL1A) and interleukin 1, beta (IL1B), and modulates a variety of interleukin 1 related immune and inflammatory responses. This gene and five other closely related cytokine genes form a gene cluster spanning approximately 400 kb on chromosome 2. A polymorphism of this gene is reported to be associated with increased risk of osteoporotic fractures and gastric cancer. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.

    • Synonyms

      IRAP, IL1F3, IL1RA, IL-1ra3, ICIL-1RA, IL1RN, IL1 inhibitor, IL-1ra, F630041P17Rik.

    • 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 MGSHMRPSGK RPCKMQAFRI WDTNQKTFYL RNNQLIAGYL QGPNIKLEEK IDMVPIDLHS VFLGIHGGKL CLSCAKSGDD IKLQLEEVNI TDLSKNKEED KRFTFIRSEK GPTTSFESAA CPGWFLCTTL EADRPVSLTN TPEEPLIVTK FYFQEDQ.

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    Il 1Ra Mouse His
  • View Data Sheet

    Description:

    Interleukin-36 Receptor Antagonist Human Recombinant

    Interleukin-36 receptor antagonist protein, FIL1 delta, IL-1-related protein 3, IL-1RP3, Interleukin-1 HY1, IL-1HY1, Interleukin-1 delta, IL-1 delta, Interleukin-1 family member 5, IL-1F5, Interleukin-1 receptor antagonist homolog 1, IL-1ra homolog 1, Interleukin-1-like protein 1, IL-1L1, IL36RN, FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, FIL1, PSORP, IL36RA, FIL1(DELTA).

    Product # :

    CYT-009

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    Description

    IL1F5 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 155 amino acids and having a molecular mass of 17kDa.The IL1F5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL1F5 was lyophilized after extensive dialysis against 20mM Phosphate buffer, pH7.4.

    Purity

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

    Biological Activity

    As measured by its binding ability in a functional ELISA, immobilized IL1F5 at 1 µg/ml (100 µl/well) can bind rHuIL-1 Rrp2/Fc Chimera with a linear range of 0.15- 5 µg/ml.

    More Info

    • Introduction

      Human interleukin family 1, member 5 (IL-1F5 / FIL1-delta) belongs to the interleukin 1 cytokine family. IL1F5 is expressed by a variety of cells including monocytes, Bcells, dendritic cells/Langerhans cells, keratinocytes,and gastric fundus Parietal and Chief cells. IL1F5 is an antagonist of IL1F9; however IL1F5 activity related to receptor binding remains unclear. Human and mouse IL1F5 share 90% amino acid sequence identity.

    • Synonyms

      Interleukin-36 receptor antagonist protein, FIL1 delta, IL-1-related protein 3, IL-1RP3, Interleukin-1 HY1, IL-1HY1, Interleukin-1 delta, IL-1 delta, Interleukin-1 family member 5, IL-1F5, Interleukin-1 receptor antagonist homolog 1, IL-1ra homolog 1, Interleukin-1-like protein 1, IL-1L1, IL36RN, FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, FIL1, PSORP, IL36RA, FIL1(DELTA).

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IL1F5 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL1F5 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 quick spin followed by reconstitution of IL1F5 in PBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Val-Leu-Ser-Gly.

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    Il1F5 Human
  • View Data Sheet

    Description:

    Interleukin-36 Receptor Antagonist Human Recombinant, His Tag

    Interleukin 36 receptor antagonist, FIL1, FIL1(DELTA), FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, IL36RA, PSORP, FIL1 delta, Interleukin-1 HY1, IL-1 delta, Interleukin-1 receptor antagonist homolog 1, Interleukin-1-like protein 1, UNQ1896/PRO4342.

    Product # :

    CYT-844

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    Description

    IL36RN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 175 amino acids (1-155 a.a) and having a molecular mass of 19.1kDa.IL36RN is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL36RN protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Human interleukin family 1, member 5 (IL-1F5 / FIL1-delta) belongs to the interleukin 1 cytokine family. IL1F5 is expressed by a variety of cells including monocytes, Bcells, dendritic cells/Langerhans cells, keratinocytes,and gastric fundus Parietal and Chief cells. IL1F5 is an antagonist of IL1F9; however IL1F5 activity related to receptor binding remains unclear. Human and mouse IL1F5 share 90% amino acid sequence identity.

    • Synonyms

      Interleukin 36 receptor antagonist, FIL1, FIL1(DELTA), FIL1D, IL1F5, IL1HY1, IL1L1, IL1RP3, IL36RA, PSORP, FIL1 delta, Interleukin-1 HY1, IL-1 delta, Interleukin-1 receptor antagonist homolog 1, Interleukin-1-like protein 1, UNQ1896/PRO4342.

    • 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 MVLSGALCFR MKDSALKVLY LHNNQLLAGG LHAGKVIKGE EISVVPNRWL DASLSPVILG VQGGSQCLSC GVGQEPTLTL EPVNIMELYL GAKESKSFTF YRRDMGLTSS FESAAYPGWF LCTVPEADQP VRLTQLPENG GWNAPITDFY FQQCD.

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    Il36Rn Human His
  • View Data Sheet

    Description:

    Serum/Glucocorticoid Regulated Kinase 1 Human Recombinant

    Serine/threonine-protein kinase Sgk1, Serum/glucocorticoid-regulated kinase 1, SGK1, SGK.

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    PKA-272

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    Description

    SGK1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (60-431 a.a.) and having a molecular mass of 44.5kDa.SGK1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SGK1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 30% glycerol, 0.2M NaCl, 2mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Serum-and glucocorticoid-regulated kinase (SGK1) is a serine/threonine protein kinase and a member of the “AGC” subfamily, which includes protein kinases A, G, and C. The SGK1 protein has an imperative role in activating specific potassium, sodium and chloride channels, suggesting a participation in the regulation of processes such as cell survival, neuronal excitability, and renal sodium excretion. SGK1 is activated in vitro by PDK-1 (3-phosphoinositide-dependent protein kinase-1) and in vivo in reaction to signals which activate phosphatidylinositol (PI) 3-kinase.

    • Synonyms

      Serine/threonine-protein kinase Sgk1, Serum/glucocorticoid-regulated kinase 1, SGK1, SGK.

    • 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 MISQPQEPEL MNANPSPPPS PSQQINLGPS SNPHAKPSDF HFLKVIGKGS FGKVLLARHK AEEVFYAVKV LQKKAILKKK EEKHIMSERN VLLKNVKHPF LVGLHFSFQT ADKLYFVLDY INGGELFYHL QRERCFLEPR ARFYAAEIAS ALGYLHSLNI VYRDLKPENI LLDSQGHIVL TDFGLCKENI EHNSTTSTFC GTPEYLAPEV LHKQPYDRTV DWWCLGAVLY EMLYGLPPFY SRNTAEMYDN ILNKPLQLKP NITNSARHLL EGLLQKDRTK RLGAKDDFME IKSHVFFSLI NWDDLINKKI TPPFNPNVSG PNDLRHFDPE FTEEPVPNSI GKSPDSVLVT ASVKEAAEAF LGFSYAPPTD SFL.

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    Sgk1 Human
  • View Data Sheet

    Description:

    HCC-1 (CCL14) Human Recombinant, His Tag

    Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.

    Product # :

    CHM-253

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    Description

    HCC-1 Human Recombinant fused with a 21 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids (20-93 a.a.) and having a molecular mass of 10.9kDa. The HCC-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HCC-1 solution (0.5 mg/ml) contains Phosphate Buffered Saline pH7.4 containing 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 14 (CCL14) is a small cytokine belonging to the CC chemokine family. It is also commonly known as HCC-1. It is produced as a protein precursor that is procesed to generate a mature active protein containing 74 amino acids that and is 46% identical in amino acid composition to CCL3 and CCL4. This chemokine is expressed in various tissues including spleen, bone marrow, liver, muscle, and gut. CCL13 activates monocytes, but does not induce their chemotaxis. Human CCL13 is located on chromosome 17 within a cluster of other chemokines belonging to the CC family.

    • Synonyms

      Small inducible cytokine A14, CCL14, Chemokine CC-1/CC-3, HCC-1/HCC-3, HCC-1(1-74), NCC-2, chemokine (C-C motif) ligand 14, CC-1, CC-3, CKb1, MCIF, SY14, HCC-1, HCC-3, SCYL2, SCYA14.

    • 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 MTKTESSSRG PYHPSECCFT YTTYKIPRQR IMDYYETNSQ CSKPGIVFIT KRGHSVCTNP SDKWVQDYIK DMKEN.

    • Background

      What is the molecular weight/Mw of CCL14 HUMAN, HIS Protein?
      CCL14 HUMAN, HIS Protein has a total Mw of 10.9kDa.

      What is the source or expression system of CCL14 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL14 HUMAN, HIS Protein?
      CCL14 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL14 HUMAN, HIS Protein?
      The biological functionality of CCL14 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL14 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MTKTESSSRG PYHPSECCFT YTTYKIPRQR IMDYYETNSQ CSKPGIVFIT KRGHSVCTNP SDKWVQDYIK DMKEN.

      What applications can CCL14 HUMAN, HIS Protein be used in?
      CCL14 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL14 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL14 HUMAN, HIS 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.

    Hcc 1 Human His
  • View Data Sheet

    Description:

    Natural Cytotoxicity Triggering Receptor 2 Human Recombinant

    Natural Cytotoxicity Triggering Receptor 2, Lymphocyte Antigen 95 (Activating NK-Receptor; NK-P44), Natural Killer Cell P44-Related Protein, NK Cell-Activating Receptor, Lymphocyte Antigen 95 Homolog, CD336 Antigen, NK-p44, LY95, dJ149M18.1.

    Product # :

    PRO-1826

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    Description

    NCR2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (19-130) and having a molecular mass of 15.0 kDa. NCR2 is fused to a 21 amino acid His-tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The NCR2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      NCR2 is a member of the natural cytotoxicity receptor (NCR) family and holds 1 immunoglobulin-like (Ig-like) domain. NCR2 cooperates with TYROBP/DAP12 and is specifically expressed by activated NK cells and by in vitro cultured TCRg/d lymphoid cells. NCR2 is a cytotoxicity-activating receptor which induces the amplified efficiency of activated natural killer (NK) cells to mediate tumor cell lysis.

    • Synonyms

      Natural Cytotoxicity Triggering Receptor 2, Lymphocyte Antigen 95 (Activating NK-Receptor; NK-P44), Natural Killer Cell P44-Related Protein, NK Cell-Activating Receptor, Lymphocyte Antigen 95 Homolog, CD336 Antigen, NK-p44, LY95, dJ149M18.1.

    • 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 MSQAQSKAQV LQSVAGQTLT VRCQYPPTGS LYEKKGWCKE ASALVCIRLV TSSKPRTMAW TSRFTIWDDP DAGFFTVTMT DLREEDSGHY WCRIYRPSDN SVSKSVRFYL VVS

    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.

    Ncr2 Human
  • View Data Sheet

    Description:

    Nephroblastoma Overexpressed Human Recombinant

    Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

    Product # :

    CYT-805

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    Description

    Nephroblastoma Overexpressed Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 331 amino acids and having a molecular mass of 36.2 kDa. The NOV is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris-HCl, pH 8.6 and 150 mM NaCl.

    Purity

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

    Biological Activity

    Determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 1.0 µg/ml, corresponding to a specific activity of > 1000 IU/mg. range of 10.0 -50.0 ng/ml, corresponding to a specific activity of 20,000-100,000units/mg.

    More Info

    • Introduction

      Nephroblastoma Overexpressed (NOV) which is encoded by the NOV gene is a part of the CCN (CTGF/CYR61/NOV) family. NOV takes part in reducing tumorgenicity and proliferation of certain cancer cell lines. NOV interacts with numerous proteins and is involved in both internal and external cell signaling. NOV is expressed in particular tumors, including Wilm’s tumor and most nephroblastomas and is also exerts proangiogenic activities.

    • Synonyms

      Protein NOV homolog, NovH, CCN family member 3, nsulin-like growth factor-binding protein 9, IBP-9, IGF-binding protein 9, IGFBP-9, Nephroblastoma-overexpressed gene protein homolog, NOV, CCN3, IGFBP9, NOVH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NOV although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NOV 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 NOV in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQVAATQRCP PQCPGRCPAT PPTCAPGVRA VLDGCSCCLV CARQRGESCS DLEPCDESSG LYCDRSADPS NQTGICTAVE GDNCVFDGVI YRSGEKFQPS CKFQCTCRDG QIGCVPRCQL DVLLPEPNCP APRKVEVPGE CCEKWICGPD EEDSLGGLTL AAYRPEATLG VEVSDSSVNC IEQTTEWTAC SKSCGMGFST RVTNRNRQCE MLKQTRLCMV RPCEQEPEQP TDKKGKKCLR TKKSLKAIHL QFKNCTSLHT YKPRFCGVCS DGRCCTPHNT KTIQAEFQCS PGQIVKKPVM VIGTCTCHTN CPKNNEAFLQ ELELKTTRGK M.

    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.

    Nov Human
  • View Data Sheet

    Description:

    BRAK (CXCL14) Rat Recombinant

    C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.

    Product # :

    CHM-021

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    Description

    CXCL14 Rat Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 77 amino acids and having a molecular mass of 9.4kDa.The CXCL14 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CXCL14 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

    Determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.

    More Info

    • Introduction

      CXCL14 is involved in immunoregulatory and inflammatory processes. BRAK protein is structurally related to the CXC (Cys-X-Cys) subfamily of cytokines. CXCL14 displays chemotactic activity for monocytes but not for lymphocytes, dendritic cells, neutrophils or macrophages. CXCL14 is involved in the homeostasis of monocyte-derived macrophages.

    • Synonyms

      C-X-C motif chemokine 14, B-cell and monocyte-activating chemokine, Chemokine BRAK, Kidney-expressed chemokine CXC, MIP-2G, Small-inducible cytokine B14, Cxcl14, Bmac, Kec, Ks1, Mip2g, Scyb14, BRAK, NJAC, AI414372, bolekine, MIP2gamma, 1110031L23Rik, 1200006I23Rik.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CXCL14 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL14 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 CXCL14 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.

    • Background

      What is the molecular weight/Mw of CXCL14 RAT Protein?
      CXCL14 RAT Protein has a total Mw of 9.4kDa.

      What is the source or expression system of CXCL14 RAT Protein?
      Escherichia Coli.

      What is the Purity of CXCL14 RAT Protein?
      CXCL14 RAT Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL14 RAT Protein?
      Determined by its ability to chemoattract activated monocytes using a concentration range of 1.0-10.0 ng/ml.

      What is the amino acid sequence of CXCL14 RAT Protein?
      SKCKCSRKGP KIRYSDVKKL EMKPKYPHCE EKMVIITTKS MSRYRGQEHC LHPKLQSTKR FIKWYNAWNE KRRVYEE.

      What applications can CXCL14 RAT Protein be used in?
      CXCL14 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL14 RAT Protein?
      The endotoxin level is minimal, CXCL14 RAT 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.

    Cxcl14 Rat
  • View Data Sheet

    Description:

    Activin-A Human Recombinant, Plant-Active

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-414

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    Description

    Active form Activin-A Human Recombinant produced in Plant is a homodimeric, glycosylated, polypeptide chain containing 2 x 116 amino acids and having a molecular weight of 27.4kDa.The Active form Activin-A is fused to a 6-His tag at N-terminus and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana.

    Formulation

    Active form Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 50mM Tris-HCl pH-7.4

    Purity

    Greater than 98% as obsereved by SDS-PAGE.

    Biological Activity

    The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.

    • Synonyms

      Inhba, Inhibin beta A, FSH releasing protein.

    • Physical Appearance

      Lyophilized freeze dried powder.

    • Stability

      For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Repeated freezing and thawing is not recommended.

    • Solubility

      INHBA protein should be reconstituted in distilled water to a concentration of 50 ug /ml. Due to the protein nature, dimmers and multimers may be observed.

    • Amino Acid Sequence

      HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSG
      YHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFA
      NLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS.

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 27.4 kDa.

      What is the source or expression system of Activin A Protein?
      Nicotiana benthamiana.

      What is the Purity of Activin A Protein?
      Activin A Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of Activin A Protein?
      The biological activity of INHBA is measured by its ability to inhibit mouse plasmacytoma cell line (MPC-11) cells proliferation ([3H]thymidine incorporation). ED50<5ng/ml.

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

      What is the amino acid sequence of ACTIVIN A Protein?HHHHHHGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCS

      What applications can ACTIVIN-A Protein be used in?

      ACTIVIN A 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.

    Activin A Active
  • View Data Sheet

    Description:

    Interleukin-7 Receptor Human Recombinant

    IL7R, Interleukin 7 Receptor, IL-7 Receptor Subunit Alpha, IL-7R Subunit Alpha,CD127 Antigen, IL-7R-Alpha, CDW127, Interleukin-7 Receptor Subunit Alpha, Interleukin 7 Receptor Isoform H5-6, Interleukin 7 Receptor Alpha Chain, IL-7RA,CD127, IL7RA, ILRA.   

    Product # :

    CYT-1046

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    Description

    IL7R produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 461 amino acids (21-239a.a.) and having a molecular mass of 52.5kDa. (Molecular size on SDS-PAGE will appear at approximately 50-70kDa). IL7R is expressed with an 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    IL7R protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Interleukin-7 receptor (IL7R) ,is a hematopoietin receptor superfamily member. IL7R takes a vital part in lymphocyte differentiation, proliferation, multiple sclerosis, as well as survival. IL7R protein signaling is vital for T-cell development and regulation of native and memory T-cell homeostasis. Likewise, IL7R is critically needed for the proper function & development of lymphoid cells.

    • Synonyms

      IL7R, Interleukin 7 Receptor, IL-7 Receptor Subunit Alpha, IL-7R Subunit Alpha,CD127 Antigen, IL-7R-Alpha, CDW127, Interleukin-7 Receptor Subunit Alpha, Interleukin 7 Receptor Isoform H5-6, Interleukin 7 Receptor Alpha Chain, IL-7RA,CD127, IL7RA, ILRA.


    • 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

      ADLESGYAQN GDLEDAELDD YSFSCYSQLE VNGSQHSLTC AFEDPDVNIT NLEFEICGAL VEVKCLNFRK LQEIYFIETK KFLLIGKSNI CVKVGEKSLT CKKIDLTTIV KPEAPFDLSV VYREGANDFV VTFNTSHLQK KYVKVLMHDV AYRQEKDENK WTHVNLSSTK LTLLQRKLQP AAMYEIKVRS IPDHYFKGFW SEWSPSYYFR TPEINNSSGE MDLEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH H

    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.

    Il7R Human
  • View Data Sheet

    Description:

    Twisted Gastrulation Protein Human Recombinant

    Twisted Gastrulation BMP Signaling Modulator 1, TSG, Twisted Gastrulation Homolog 1 (Drosophila), Twisted Gastrulation Protein Homolog 1, Twisted Gastrulation Homolog 1, TWSG1.

    Product # :

    CYT-873

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    Description

    TWSG1 Human Recombinant (26-223) produced in CHO is a single, glycosylated, polypeptide chain containing 198 amino acids and having a molecular mass ranging from 35-43kDa on SDS-PAGE due to glycosylation.The TWSG1 is purified by proprietary chromatographic techniques.

    Source

    CHO.

    Formulation

    Lyophilized from a 0.2µm filtered solution in PBS.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50, as measured by its ability to inhibit alkaline phosphatase production induced by rHuBMP-6 in mouse ATDC5 cells, is less than 16µg/ml.

    More Info

    • Introduction

      Twisted gastrulation Protein (TSG) is a secreted, cysteine-rich protein which has a role in dorsal/ventral patterning in Drosophila and Xenopus by regulating BMP signaling. TSG functions as an agonist for BMP signaling by controlling the inhibitory actions of the BMP antagonist, Chordin/Sog, and the cleavage properties of the metalloprotease, xolloid/tolloid. TSG N-terminal domain binds BMP protein directly and displays BMP antagonist activity.

    • Synonyms

      Twisted Gastrulation BMP Signaling Modulator 1, TSG, Twisted Gastrulation Homolog 1 (Drosophila), Twisted Gastrulation Protein Homolog 1, Twisted Gastrulation Homolog 1, TWSG1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TSG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TSG 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 TSG in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      CNKALCASDV SKCLIQELCQ CRPGEGNCSC CKECMLCLGA LWDECCDCVG MCNPRNYSDT PPTSKSTVEE LHEPIPSLFR ALTEGDTQLN WNIVSFPVAE ELSHHENLVS FLETVNQPHH QNVSVPSNNV HAPYSSDKEH MCTVVYFDDC MSIHQCKISC ESMGASKYRW FHNACCECIG PECIDYGSKT VKCMN CMF.

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    Tsg Human
  • View Data Sheet

    Description:

    Hexarelin

    Product # :

    HOR-288

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    Description

    Hexarelin has 7 amino acids H-His-D-2-Methyl-Trp-Ala-Trp-D-Phe-Lys-NH2 and having a molecular weight of 887 Dalton. The Molecular Formula is C47H58N12O6.

    Formulation

    The Hexarelin peptide was lyophilized with no additives.

    Purity

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

    More Info

    • Introduction

      Hexarelin stimulates GH secretion. Hexarelin is more resistant to proteolytic degradation than GHRP-6.

    • Physical Appearance

      Sterile Filtered lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Hexarelin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Hexarelin 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 Hexarelin 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Hexarelin