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  • View Data Sheet

    Description:

    Mucosae-Associated Epithelial Chemokine (CCL28) Rat Recombinant

    MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    Product # :

    CHM-278

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    Description

    MEC Rat Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13.1kDa. The Rat MEC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH 7.4 and150mM NaCl.

    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 murine lymphocytes using a concentration range of 1.0-10.0 ng/ml.

    More Info

    • Introduction

      CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
      Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.

    • Synonyms

      MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SEAILPIASS CCTEVSHHIP RRLLERVNSC SIQRADGDCD LAAVILHVKR RRICVSPHNP TLKRWMSASE MKNGKENLCP RKKQDSGKDR KGHTPRKHGK HGTRRIHGTH DHEAPR.

    • Background

      What is the molecular weight/Mw of CCL28 RAT Protein?
      CCL28 RAT Protein has a total Mw of 13.1kDa.

      What is the source or expression system of CCL28 RAT Protein?
      Escherichia Coli.

      What is the Purity of CCL28 RAT Protein?
      CCL28 RAT Protein is > 95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL28 RAT Protein?
      Determined by its ability to chemoattract murine lymphocytes using a concentration range of 1.0-10.0 ng/ml.

      What is the amino acid sequence of CCL28 RAT Protein?
      SEAILPIASS CCTEVSHHIP RRLLERVNSC SIQRADGDCD LAAVILHVKR RRICVSPHNP TLKRWMSASE MKNGKENLCP RKKQDSGKDR KGHTPRKHGK HGTRRIHGTH DHEAPR.

      What applications can CCL28 RAT Protein be used in?
      CCL28 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL28 RAT Protein?
      The endotoxin level is minimal, CCL28 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.

    Ccl28 Rat
  • View Data Sheet

    Description:

    Fractalkine Rat Recombinant (CX3CL1)

    Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    Product # :

    CHM-005

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    Description

    Fractalkine Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids and having a molecular mass of 8.7kDa.The Fractalkine is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    Determined by its ability to chemoattract human monocytes using a concentration range of 5.0-10.0 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

    More Info

    • Introduction

      Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Natural Human Fractalkine is produced as a long protein (373-amino acid) with an extended mucin-like stalk and a chemokine domain on top. The mucin-like stalk permits it to bind to the cell surface. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

    • Synonyms

      Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QHLGMTKCNI TCHKMTSPIP VTLLIHYQLN QESCGKRAII LETRQHRHFC ADPKEKWVQD AMKHLDHQTA ALTRNG

    • Background

      What is the molecular weight/Mw of CX3CL1 RAT Protein?
      CX3CL1 RAT Protein has a total Mw of 8.7kDa.

      What is the source or expression system of CX3CL1 RAT Protein?
      Escherichia Coli.

      What is the Purity of CX3CL1 RAT Protein?
      CX3CL1 RAT Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CX3CL1 RAT Protein?
      Determined by its ability to chemoattract human monocytes using a concentration range of 5.0-10.0 ng/ml, corresponding to a specific activity of 100,000-200,000units/mg.

      What is the amino acid sequence of CX3CL1 RAT Protein?
      QHLGMTKCNI TCHKMTSPIP VTLLIHYQLN QESCGKRAII LETRQHRHFC ADPKEKWVQD AMKHLDHQTA ALTRNG

      What applications can CX3CL1 RAT Protein be used in?
      CX3CL1 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CX3CL1 RAT Protein?
      The endotoxin level is minimal, CX3CL1 RAT Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CX3CL1 RAT that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CX3CL1 RAT?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Fractalkine Rat
  • View Data Sheet

    Description:

    Globular Adiponectin Mouse Recombinant

    Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    Product # :

    CYT-432

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    • sds-page

    Description

    The globular domain of Adiponectin Mouse Recombinant / Acrp30 Mouse contains 138 amino acid residues from a.a. 111-247 having molecular mass of 16 kDa was over expressed in E.coli and purified by using conventional chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    Acrp30 Mouse (1mg/ml) solution containing 20mM Tris-HCl pH7.5, 50mM NaCl, 5mM DTT and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    More Info

    • Introduction

      Adiponectin (247amino acids) is adipocyte complement-related protein of 30 kDa and exclusively expressed in differentiated adipocytes. APM-1 (Acrp30 Mouse) is a member of the complement factor C1q family and consists of signal sequence, Non-homologous sequence, collagen domain and domain (gAcrp30).
      Adiponectin expression is reduced in a variety of obese and insulin-resistant states in human, monkeys and mice. Injection of Acrp30 Mouse (247aa) or gAcrp30 (globular domain) lowers serum glucose and free fatty acid level in mice.

    • Synonyms

      Acrp30, AdipoQ, GBP-28, APM-1, ACDC.

    • 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

      MAYMYRSAFS VGLETRVTVP NVPIRFTKIF YNQQNHYDGS TGKFYCNIPG LYYFSYHITVYMKDVKVSLF KKDKAVLFTY DQYQEKNVDQ ASGSVLLHLE VGDQVWLQVY GDGDHNGLYADNVNDSTFTG FLLYHDTN

    • Background

      What is the molecular weight/Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 16kDa.

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

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

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

      What is the amino acid sequence of ADIPONECTIN Protein?
      MAYMYRSAFS VGLETRVTVP NVPIRFTKIF YNQQNHYDGS TGKFYCNIPG LYYFSYHITVYMKDVKVSLF KKDKAVLFTY DQYQEKNVDQ ASGSVLLHLE VGDQVWLQVY GDGDHNGLYADNVNDSTFTG FLLYHDTN

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

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

    Adiponectin Globular Mouse
  • View Data Sheet

    Description:

    TYRO3 Protein Tyrosine Kinase Mouse Recombinant

    Etk2/tyro3, TK19-2, Tyrosine-protein kinase DTK, Tyrosine-protein kinase RSE, Tyrosine-protein kinase TIF, Tyro3, Dtk, Rse, Tif, AI323366, Brt, Etk-2.

    Product # :

    PKA-120

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    Description

    TYRO3 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 628 amino acids (31-419 aa) and having a molecular mass of 68.9kDa.TYRO3 is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The TYRO3 solution (0.25mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      TYRO3 Protein Tyrosine Kinase or TYRO3 is a transmembrane receptor tyrosine kinase. TYRO3 has crucial role in essential processes such as cell migration, actin reorganization and cell survival. It is activated and signaled by MAPK/ERK and PI3K/AKT that expedites the cellular functions of protein.

    • Synonyms

      Etk2/tyro3, TK19-2, Tyrosine-protein kinase DTK, Tyrosine-protein kinase RSE, Tyrosine-protein kinase TIF, Tyro3, Dtk, Rse, Tif, AI323366, Brt, Etk-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

      AGLKLMGAPV KMTVSQGQPV KLNCSVEGME DPDIHWMKDG TVVQNASQVS ISISEHSWIG LLSLKSVERS DAGLYWCQVK DGEETKISQS VWLTVEGVPF FTVEPKDLAV PPNAPFQLSC EAVGPPEPVT IYWWRGLTKV GGPAPSPSVL NVTGVTQRTE FSCEARNIKG LATSRPAIVR LQAPPAAPFN TTVTTISSYN ASVAWVPGAD GLALLHSCTV QVAHAPGEWE ALAVVVPVPP FTCLLRNLAP ATNYSLRVRC ANALGPSPYG DWVPFQTKGL APARAPQNFH AIRTDSGLIL EWEEVIPEDP GEGPLGPYKL SWVQENGTQD ELMVEGTRAN LTDWDPQKDL ILRVCASNAI GDGPWSQPLV VSSHDHAGRQ GPPHSRTSWL EPKSCDKTHT CPPCPAPELL GGPSVFLFPP KPKDTLMISR TPEVTCVVVD VSHEDPEVKF NWYVDGVEVH NAKTKPREEQ YNSTYRVVSV LTVLHQDWLN GKEYKCKVSN KALPAPIEKT ISKAKGQPRE PQVYTLPPSR DELTKNQVSL TCLVKGFYPS DIAVEWESNG QPENNYKTTP PVLDSDGSFF LYSKLTVDKS RWQQGNVFSC SVMHEALHNH YTQKSLSLSP GKHHHHHH

    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.

    Tyro3 Mouse
  • View Data Sheet

    Description:

    GRO-beta/MIP-2 Rat 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, CINC-3.

    Product # :

    CHM-372

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    Description

    GRO-Beta Rat Recombinant also called Rat MIP-2 produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7923 Dalton. The GRO-b is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 99.0% as determined 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 100,000-1,000,000 units/mg.

    More Info

    • 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, CINC-3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized GRO-b 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 Rat in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      VVVASELRCQ CLTTLPRVDF KNIQSLTVTP PGPHCAQTEV IATLKDGHEV CLNPEAPLVQ RIVQKILNKG KAN.

    • Background

      What is the molecular weight/Mw of CXCL2 RAT Protein?
      CXCL2 RAT Protein has a total Mw of 7.92kDa.

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

      What is the Purity of CXCL2 RAT Protein?
      CXCL2 RAT Protein is >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL2 RAT 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 100,000-1,000,000 units/mg.

      What is the amino acid sequence of CXCL2 RAT Protein?
      VVVASELRCQ CLTTLPRVDF KNIQSLTVTP PGPHCAQTEV IATLKDGHEV CLNPEAPLVQ RIVQKILNKG KAN.

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

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

      Who supplies recombinant CXCL2 RAT that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CXCL2 RAT?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Gro B Rat
  • View Data Sheet

    Description:

    V-ral Simian Leukemia Viral Oncogene Homolog A Mouse Recombinant

    Ras-related protein Ral-A, Rala, Ral, Ral-a, RALA. 

    Product # :

    PRO-2497

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    Description

    RALA Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-203 a.a) and having a molecular mass of 25.7kDa. RALA is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RALA protein solution (0.5mg/ml) 20mM Tris-Hcl buffer (pH8.5) containing 30% glycerol, 0.1M NaCl and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ras-related protein Ral-A (RALA) is a member of the small GTPase superfamily, Ras family of proteins. RALA mediates a distinct downstream signaling pathway from Ras which facilitates cellular transformation. Furthermore, RALA is thought to be involved in various signaling cascades, including regulation of the cytoskeleton, vesicle trafficking, and endocytosis.

    • Synonyms

      Ras-related protein Ral-A, Rala, Ral, Ral-a, RALA.

    • 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 MGSHMAANKP KGQNSLALHK VIMVGSGGVG KSALTLQFMY DEFVEDYEPT KADSYRKKVV LDGEEVQIDI LDTAGQEDYA AIRDNYFRSG EGFLCVFSIT EMESFAATAD FREQILRVKE DENVPFLLVG NKSDLEDKRQ VSVEEAKNRA DQWNVNYVET SAKTRANVDK VFFDLMREIR ARKMEDSKEK NGKKKRKSLA KRIRERC

    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.

    Rala Mouse
  • View Data Sheet

    Description:

    RAN Guanine Nucleotide Release Factor Human Recombinant

    Ran guanine nucleotide release factor, RanGNRF, Ran-binding protein MOG1, RANGRF, MOG1, HSPC165, HSPC236, MDS5.

    Product # :

    PRO-1149

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    Description

    RANGRF Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids (1-186 a.a) and having a molecular mass of 23kDa.RANGRF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RANGRF protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      RANGRF is a protein which acts as a guanine nucleotide release factor in mouse and regulates the expression and function of the Nav1.5 cardiac sodium channel in human. RANGRF also controls the intracellular trafficking of RAN. In cardiac cells, the RANGRF appears to regulate the cell surface localization of SCN5A.

    • Synonyms

      Ran guanine nucleotide release factor, RanGNRF, Ran-binding protein MOG1, RANGRF, MOG1, HSPC165, HSPC236, MDS5.

    • 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 MGSHMEPTRD CPLFGGAFSA ILPMGAIDVS DLRPVPDNQE VFCHPVTDQS LIVELLELQA HVRGEAAARY HFEDVGGVQG ARAVHVESVQ PLSLENLALR GRCQEAWVLS GKQQIAKENQ QVAKDVTLHQ ALLRLPQYQT DLLLTFNQPP PDNRSSLGPE NLSPAPWSLG DFEQLVTSLT LHDPNIFGPQ.

    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.

    Rangrf Human
  • View Data Sheet

    Description:

    Rantes Rhesus Macaque Recombinant (CCL5)

    C-C motif chemokine 5, Small-inducible cytokine A5, T-cell-specific protein RANTES, CCL5.

    Product # :

    CHM-033

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    Description

    Rantes Rhesus Macaque Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7.8kDa.The CCL5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Rantes protein was lyophilized from a 0.2µm filtered concentrated solution in 20mM PB pH 6.0 and 500mM NaCl.

    Purity

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

    Biological Activity

    The biological activity determined by a chemotaxis bioassay using human peripheral blood monocytes is in a concentration range of 1.0-10 ng/ml.

    More Info

    • Introduction

      Regulated upon Activation, Normal T-cell Expressed, and Secreted or RANTES is an 8 kDa protein classified as a chemotactic cytokine or chemokine. It has recently been renamed CCL5. RANTES is chemotactic for T cells, eosinophils and basophils and plays an active role in recruiting leukocytes into inflammatory sites. With the help of particular cytokines (i.e. IL-2 and IFN-?) that are released by T cells, RANTES also induces the proliferation and activation of certain natural killer (NK) cells to form CHAK (CC-Chemokine-activated killer) cells. It is also a HIV-suppressive factor released from CD8+ T cells. This chemokine has been localized to chromosome 17 in humans.

    • Synonyms

      C-C motif chemokine 5, Small-inducible cytokine A5, T-cell-specific protein RANTES, CCL5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Rantes although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL5 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 Rantes in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPHASDTTPC CFAYIARPLP RAHIKEYFYT SGKCSNPAVV FVTRKNRQVC ANPEKKWVRE YINSLEMS.

    • Background

      What is the molecular weight/Mw of CCL5 RHESUS MACAQUE Protein?
      CCL5 RHESUS MACAQUE Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CCL5 RHESUS MACAQUE Protein?
      Escherichia Coli.

      What is the Purity of CCL5 RHESUS MACAQUE Protein?
      CCL5 RHESUS MACAQUE Protein is > 98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL5 RHESUS MACAQUE Protein?
      The biological activity determined by a chemotaxis bioassay using human peripheral blood monocytes is in a concentration range of 1.0-10 ng/ml.

      What is the amino acid sequence of CCL5 RHESUS MACAQUE Protein?
      SPHASDTTPC CFAYIARPLP RAHIKEYFYT SGKCSNPAVV FVTRKNRQVC ANPEKKWVRE YINSLEMS.

      What applications can CCL5 RHESUS MACAQUE Protein be used in?
      CCL5 RHESUS MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL5 RHESUS MACAQUE Protein?
      The endotoxin level is minimal, CCL5 RHESUS MACAQUE Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CCL5 RHESUS MACAQUE that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CCL5 RHESUS MACAQUE?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Rantes Rhesus Macaque
  • View Data Sheet

    Description:

    Ring Finger Protein 7 Human Recombinant

    RING-box protein 2 isoform 1, Ring finger protein 7, CKBBP1, ROC2, SAG, RING-box protein 2, Rbx2, CKII beta-binding protein 1, Regulator of cullins 2, Sensitive to apoptosis gene protein, RBX2, RNF7.

    Product # :

    PRO-1671

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    Description

    RNF7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 136 amino acids (1-113 a.a) and having a molecular mass of 15.1kDa.RNF7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RNF7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ring Finger Protein 7, also known as RNF7, is an extremely conserved ring finger protein. RNF7 is a vital subunit of SKP1-cullin/CDC53-F box protein ubiquitin ligases that are a part of the protein degradation machinery important for cell cycle progression and signal transduction. RNF7 is a substrate of casein kinase II (CSNK2A1/CKII) and also interacts with it. The phosphorylation of RNF7 by CSNK2A1 promotes the degradation of IkappaBalpha (CHUK/IKK-alpha/IKBKA) and p27Kip1(CDKN1B).

    • Synonyms

      RING-box protein 2 isoform 1, Ring finger protein 7, CKBBP1, ROC2, SAG, RING-box protein 2, Rbx2, CKII beta-binding protein 1, Regulator of cullins 2, Sensitive to apoptosis gene protein, RBX2, RNF7.

    • 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 MGSMADVEDG EETCALASHS GSSGSKSGGD KMFSLKKWNA VAMWSWDVEC DTCAICRVQV MDACLRCQAE NKQEDCVVVW GECNHSFHNC CMSLWVKQNN RCPLCQQDWV VQRIGK.

    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.

    Rnf7 Human
  • View Data Sheet

    Description:

    Granulocyte Macrophage-Colony Stimulating Factor Mouse Recombinant

    CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF

    Product # :

    CYT-222

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    Description

    Granulocyte Macrophage Colony Stimulating Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids and having a molecular mass of 14285.35 Dalton.GM-CSF Mouse is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GM-CSF Mouse was lyophilized with no additives.

    Purity

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

    Biological Activity

    The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

    More Info

    • Introduction

      GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
      GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

    • Synonyms

      CSF-2, MGI-1GM, GM-CSF, Pluripoietin-alpha, CSF2, GMCSF

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Granulocyte Macrophage Colony Stimulating Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GM-CSF 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 Granulocyte Macrophage Colony Stimulating Factor in sterile 20mM AcOH (acetic Acid) 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 was determined and was found to be Met-Ala-Pro-Thr-Arg.

    • Background

      What is the molecular weight/Mw of GM-CSF MOUSE Protein?
      GM-CSF MOUSE Protein has a total Mw of 14.28kDa.

      What is the source or expression system of GM-CSF MOUSE Protein?
      Escherichia Coli.

      What is the Purity of GM-CSF MOUSE Protein?
      GM-CSF MOUSE Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of GM-CSF MOUSE Protein?
      The ED50 as determined by the dose-dependant stimulation of the proliferation of murine FDC-P1 cell line is < 0.2 ng/ml, corresponding to a Specific Activity of 5,000,000 IU/mg.

      What is the amino acid sequence of GM-CSF MOUSE Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Met-Ala-Pro-Thr-Arg.

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

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


    • Protein content

      GM-CSF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.765 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 GM-CSF 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.

    Gm Csf Mouse
  • View Data Sheet

    Description:

    Interleukin 12 Receptor Beta 1 Human Recombinant

    Interleukin 12 Receptor Beta 1, IL-12 Receptor Beta Component, IL-12 Receptor Subunit Beta-1, IL-12R Subunit Beta-1, IL12RB, Interleukin-12 Receptor Subunit Beta-1, Interleukin-12 Receptor Beta-1 Chain, Cluster Of Differentiation 212, CD212 Antigen, IL-12R-Beta-1, IL-12R-BETA1, IL-12RB1, CD212, IMD30, IL12R.

    Product # :

    CYT-862

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    Description

    IL12RB1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 568 amino acids (1-545 a.a) and having a molecular mass of 62.6kDa. IL12RB1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    IL12RB1 protein solution (0.25mg/ml) containing 20mM TRIS 8.0 buffer and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    More Info

    • Introduction

      IL-12 is a heterodimeric cytokine that stimulates the production of IFN gamma from T-cells and natural killer cells, and also induces differentiation of Th1 helper cells. It is an initiator of cell-mediated immunity.

    • Synonyms

      Interleukin 12 Receptor Beta 1, IL-12 Receptor Beta Component, IL-12 Receptor Subunit Beta-1, IL-12R Subunit Beta-1, IL12RB, Interleukin-12 Receptor Subunit Beta-1, Interleukin-12 Receptor Beta-1 Chain, Cluster Of Differentiation 212, CD212 Antigen, IL-12R-Beta-1, IL-12R-BETA1, IL-12RB1, CD212, IMD30, IL12R.

    • 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 MGSMEPLVTW VVPLLFLFLL SRQGAACRTS ECCFQDPPYP DADSGSASGP RDLRCYRISS DRYECSWQYE GPTAGVSHFL RCCLSSGRCC YFAAGSATRL QFSDQAGVSV LYTVTLWVES WARNQTEKSP EVTLQLYNSV KYEPPLGDIK VSKLAGQLRM EWETPDNQVG AEVQFRHRTP SSPWKLGDCG PQDDDTESCL CPLEMNVAQE FQLRRRQLGS QGSSWSKWSS PVCVPPENPP QPQVRFSVEQ LGQDGRRRLT LKEQPTQLEL PEGCQGLAPG TEVTYRLQLH MLSCPCKAKA TRTLHLGKMP YLSGAAYNVA VISSNQFGPG LNQTWHIPAD THTEPVALNI SVGTNGTTMY WPARAQSMTY CIEWQPVGQD GGLATCSLTA PQDPDPAGMA TYSWSRESGA MGQEKCYYIT IFASAHPEKL TLWSTVLSTY HFGGNASAAG TPHHVSVKNH SLDSVSVDWA PSLLSTCPGV LKEYVVRCRD EDSKQVSEHP VQPTETQVTL SGLRAGVAYT VQVRADTAWL RGVWSQPQRF SIEVQVSD.

    • Background

      What is the molecular weight/Mw of IL12RB1 HUMAN Protein?
      IL12RB1 HUMAN Protein has a total Mw of 62.6kDa.

      What is the source or expression system of IL12RB1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IL12RB1 HUMAN Protein?
      IL12RB1 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of IL12RB1 HUMAN Protein?
      The biological functionality of IL12RB1 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IL12RB1 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMEPLVTW VVPLLFLFLL SRQGAACRTS ECCFQDPPYP DADSGSASGP RDLRCYRISS DRYECSWQYE GPTAGVSHFL RCCLSSGRCC YFAAGSATRL QFSDQAGVSV LYTVTLWVES WARNQTEKSP EVTLQLYNSV KYEPPLGDIK VSKLAGQLRM EWETPDNQVG AEVQFRHRTP SSPWKLGDCG PQDDDTESCL CPLEMNVAQE FQLRRRQLGS QGSSWSKWSS PVCVPPENPP QPQVRFSVEQ LGQDGRRRLT LKEQPTQLEL PEGCQGLAPG TEVTYRLQLH MLSCPCKAKA TRTLHLGKMP YLSGAAYNVA VISSNQFGPG LNQTWHIPAD THTEPVALNI SVGTNGTTMY WPARAQSMTY CIEWQPVGQD GGLATCSLTA PQDPDPAGMA TYSWSRESGA MGQEKCYYIT IFASAHPEKL TLWSTVLSTY HFGGNASAAG TPHHVSVKNH SLDSVSVDWA PSLLSTCPGV LKEYVVRCRD EDSKQVSEHP VQPTETQVTL SGLRAGVAYT VQVRADTAWL RGVWSQPQRF SIEVQVSD.
      What applications can IL12RB1 HUMAN Protein be used in?
      IL12RB1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IL12RB1 HUMAN Protein?
      The endotoxin level is minimal, IL12RB1 HUMAN Protein was purified using conventional chromatography techniques.

      Who supplies recombinant IL12RB1 HUMAN that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of IL12RB1 HUMAN?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Il12Rb1 Human
  • View Data Sheet

    Description:

    Epiregulin Human Recombinant

    EREG, Epiregulin, ER.

    Product # :

    CYT-609

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    Description

    Epiregulin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 49 amino acids and having a molecular mass of 5.6 kDa. Epiregulin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Epiregulin was lyophilized from 0.5mg/ml solution ciontaing 20mM PBS buffer pH-7.4 containing 20mM sodium chloride.

    Purity

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

    Biological Activity

    The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.

    More Info

    • Introduction

      Epiregulin is part of the EGF family. Epiregulin functions as a ligand of EGFR, as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors.Epiregulin is expressed mostly in the placenta and peripheral blood leukocytes and in specific carcinomas of the bladder, lung, kidney and colon. Epiregulin stimulates the proliferation of keratinocytes, hepatocytes, fibroblasts and vascular smooth muscle cells. Epiregulin inhibits the growth of several tumor-derived epithelial cell lines. Human Epiregulin is initially synthesized as a glycosylated 19.0 kDa transmembrane precursor protein, which is processed by proteolytic cleavage to produce a 6.0 kDa mature secreted sequence.

    • Synonyms

      EREG, Epiregulin, ER.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.

    • Background

      What is the molecular weight/Mw of EREG Protein?
      EREG Protein has a total Mw of 5.6kDa.

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

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

      What is the Biological Activity of EREG Protein?
      The ED50 was determined by the dose-dependent stimulation of the proliferation of murine Balb/3T3 cells is < 2.0 ng/ml, corresponding to a specific activity of > 500,000 units/mg.

      What is the amino acid sequence of EREG Protein?
      VAQVSITKC SSDMNGYCLH GQCIYLVDMS QNYCRCEVGY TGVRCEHFFL.

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

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

    Epiregulin Human
  • View Data Sheet

    Description:

    Epidermal Growth Factor Human Recombinant, Pichia

    Urogastrone, URG, EGF.

    Product # :

    CYT-332

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    Description

    Epidermal Growth Factor Human Recombinant produced in Pichia Pastoris is a single, glycosylated, polypeptide chain containing 51 amino acids and having a molecular mass of 6KDa.The EGF is purified by proprietary chromatographic techniques.

    Source

    Pichia Pastoris.

    Formulation

    Lyophilized from a filtered concentrated solution in PBS, pH 7.4.

    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 BALB/c 3T3 cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 107 Units/mg.

    More Info

    • Introduction

      Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide. EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.

    • Background

      Harnessing Pichia for Epidermal Growth Factor Human Recombinant Production: Novel Approaches and Therapeutic Implications

      Abstract:

      This research paper delves into a cutting-edge avenue of Epidermal Growth Factor (EGF) Human Recombinant production by leveraging Pichia as an expression host. Through a synthesis of advanced methodologies encompassing genetic engineering, fermentation, and bioinformatics, this study explores the potential of Pichia-based platforms for enhanced EGF yield and biological activity. The findings not only offer insights into efficient EGF production but also underscore the therapeutic prospects of this approach.

      Introduction:

      Epidermal Growth Factor (EGF) holds a crucial place in cellular processes. This paper explores a novel dimension of EGF Human Recombinant production utilizing Pichia expression systems, emphasizing both technical aspects and the potential impact on therapeutic applications.

      Pichia as an Expression Host:

      Pichia stands as a promising alternative to conventional expression platforms due to its robustness and eukaryotic machinery. This paper investigates the strategic integration of EGF gene into Pichia, utilizing tailored vectors and promoters for optimal protein production.

      Genetic Engineering Strategies:

      Precise genetic manipulation is pivotal for enhanced EGF yield. Gene codon optimization and signal peptide selection are meticulously undertaken to ensure proper protein folding and secretion in Pichia. Through these approaches, EGF expression and secretion are finely tuned, resulting in biologically active EGF.

      Fermentation and Protein Purification:

      Expression is followed by fermentation in controlled conditions, leading to EGF accumulation. This step is supplemented by purification processes like chromatography, ensuring high EGF purity. Biochemical assays validate the biological activity of the purified EGF, affirming its therapeutic potential.

      Bioinformatics in EGF-Pichia Interaction:

      Advanced bioinformatics analyses shed light on the intricate interactions between EGF and Pichia host. Structural modeling and molecular dynamics simulations provide insights into potential post-translational modifications and protein-protein interactions, enriching our understanding of EGF behavior in Pichia.

      Therapeutic Implications:

      Beyond production, the paper emphasizes the therapeutic significance of EGF produced in Pichia. Enhanced production efficiency directly impacts cost-effectiveness, broadening its accessibility for therapeutic use. The EGF-Pichia approach presents exciting avenues for wound healing therapies and targeted cancer interventions.

      Challenges and Future Directions:

      Despite the progress, challenges such as glycosylation patterns and scaling-up strategies remain. Future efforts should focus on refining glycosylation profiles to ensure consistent bioactivity and optimizing bioreactor designs to scale up production for clinical applications.

      Conclusion:

      In a synergy of advanced methodologies and therapeutic implications, the Pichia-based Epidermal Growth Factor Human Recombinant production presents an innovative paradigm. The intricate harmony between Pichia host and EGF production holds promise for novel therapies, underscoring the potential impact of this pioneering approach.

      What is the molecular weight/Mw of EGF Protein?
      EGF Protein has a total Mw of 6kDa.

      What is the source or expression system of EGF Protein?
      Pichia Pastoris.

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

      What is the Biological Activity of EGF Protein?
      The ED₅₀, calculated by the dose-dependant proliferation of murine BALB/c 3T3 cells (measured by 3H-thymidine uptake) is < 0.1 ng/ml corresponding to a specific activity of 1 x 107 Units/mg.

      What is the amino acid sequence of EGF Protein?
      NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.

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

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

    Egf Human Pichia
  • View Data Sheet

    Description:

    Insulin Like Growth Factor-1, Mutant E3R Human Recombinant

    Insulin-Like Growth Factor-1.

    Product # :

    CYT-1217

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    Description

    IGF1 E3R Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids (Gly49-Ala118) and having a molecular mass of 8.6kDa. IGF1 E3R Human is fused to a 6 a.a his tag at C-Terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The filtered (0.4µm) concentrated protein solution was lyophilized from 0.5mg/ml solution in 50 mM NaCl, 20 mM Tris and 5% (w/v) trehalose, pH 8.0.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Insulin-Like Growth Factor-1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. IGF1 E3R is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MGPRTLCGAE LVDALQFVCG DRGFYFNKPT GYGSSSRRAP QTGIVDECCF RSCDLRRLEM YCAPLKPAKS AHHHHHH.

    • Background

      Insulin-like Growth Factor 1 (IGF-1) is a critical peptide hormone that plays a central role in regulating growth and development. Genetic mutations in the IGF-1 gene can result in altered IGF-1 variants, leading to various physiological consequences. Understanding these IGF-1 mutants is of paramount importance as they offer insights into growth disorders, metabolic regulation, and potential therapeutic avenues. This research delves into the world of IGF-1 mutants, shedding light on their diverse functions and implications for human health.

      The primary objective of this research is to elucidate the impact of IGF-1 mutations on growth regulation. In vitro and in vivo experiments will be conducted to investigate how these mutants interact with IGF-1 receptors, influence downstream signaling pathways, and modulate growth plate dynamics. Understanding these mechanisms is crucial for unraveling the complexities of growth disorders associated with IGF-1 mutations.

      The second objective is to assess the clinical relevance of IGF-1 mutants in growth-related conditions. Clinical studies involving individuals with growth hormone deficiencies or growth disorders linked to IGF-1 mutations will be conducted to evaluate the effects of these mutants on stature and overall health. These investigations may provide valuable insights into potential therapeutic strategies for individuals affected by growth-related disorders.

      The third objective is to explore the broader implications of IGF-1 mutants in metabolic regulation and age-related conditions. Research will investigate their roles in metabolic homeostasis, longevity, and susceptibility to age-related diseases. Understanding the multifaceted properties of IGF-1 mutants may open new avenues for therapeutic interventions in various health and aging-related conditions.

      By delving into the diverse functions of IGF-1 mutants, this research aims to expand our understanding of their physiological roles and clinical applications. The findings may contribute to the development of targeted interventions for growth disorders, metabolic conditions, and age-related diseases.

      What is the molecular weight/Mw of IGF1 E3R HUMAN Protein?
      IGF1 E3R HUMAN Protein has a total Mw of 8.6kDa.

      What is the source or expression system of IGF1 E3R HUMAN Protein?
      Escherichia Coli.

      What is the Purity of IGF1 E3R HUMAN Protein?
      IGF1 E3R HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IGF1 E3R HUMAN Protein?
      The biological functionality of IGF1 E3R HUMAN Protein will be determined in the future.

      What is the amino acid sequence of IGF1 E3R HUMAN Protein?
      MGPRTLCGAE LVDALQFVCG DRGFYFNKPT GYGSSSRRAP QTGIVDECCF RSCDLRRLEM YCAPLKPAKS AHHHHHH.

      What applications can IGF1 E3R HUMAN Protein be used in?
      IGF1 E3R HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IGF1 E3R HUMAN Protein?
      The endotoxin level is minimal, IGF1 E3R 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.

    Igf1 Mutant
  • View Data Sheet

    Description:

    E-Selectin, Mouse Anti-Human

    E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.

    Product # :

    ANT-237

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    Formulation

    1mg/ml in PBS (after reconstitution).

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    • Introduction

      E-Selectin belongs to a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. CD62E is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. CD62E is found in cytokine-stimulated endothelial cells and is accountable for the accumulation of blood leukocytes at sites of inflammation by mediating the adhesion of cells to the vascular lining. It demonstrates structural features such as the existence of lectin- and EGF-like domains followed by short consensus repeat (SCR) domains that contain 6 conserved cysteine residues. E-Selectin participates in the interaction between leukocytes and the endothelium and appears to be involved in the pathogenesis of atherosclerosis.

    • Synonyms

      E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E.

    • Solubility

      Reconstitute with of H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.

    • Immunogen

      Purified, Activated T-Cells.

    • Ig Subclass

      Mouse IgG1.

    • Clone

      hCD62E.

    • Applications

      Staining antibody. For staining, use 10µl/1,000,000 cells.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      Lyophilized: store at 4 C. After reconstitution, if not intended for use within a month, aliquot and store at -20 C.

    • Purification Method

      Ion exchange column.

    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.

    Cd62E Antibody
  • View Data Sheet

    Description:

    Maltose Binding Protein E.coli Recombinant, His Tag

    Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

    Product # :

    PRO-2322

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    Description

    Recombinant E.Coli MBP produced in E.Coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (27-392 a.a) and having a molecular mass of 44.9kDa. MBP is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Maltose Binding Protein is a member of the maltose/maltodextrin system of E.Coli, which is accountable for the uptake and efficient catabolism of maltodextrins. The maltose/maltodextrin is a complex regulatory and transport system involving many proteins and protein complexes.
      MBP elevates the yield of its fusion partner in many cases and is often able to promote the solubility of polypeptides to which it is fused.

    • Synonyms

      Maltose-binding periplasmic protein, MBP, MMBP, Maltodextrin-binding protein, malE, b4034, JW3994.

    • 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 MGSMKIEEGK LVIWINGDKG YNGLAEVGKK FEKDTGIKVT VEHPDKLEEK FPQVAATGDG PDIIFWAHDR FGGYAQSGLL AEITPDKAFQ DKLYPFTWDA VRYNGKLIAY PIAVEALSLI YNKDLLPNPP KTWEEIPALD KELKAKGKSA LMFNLQEPYF TWPLIAADGG YAFKYENGKY DIKDVGVDNA GAKAGLTFLV DLIKNKHMNA DTDYSIAEAA FNKGETAMTI NGPWAWSNID TSKVNYGVTV LPTFKGQPSK PFVGVLSAGI NAASPNKELA KEFLENYLLT DEGLEAVNKD KPLGAVALKS YEEELAKDPR IAATMENAQK GEIMPNIPQM SAFWYAVRTA VINAASGRQT VDEALKDAQT NSSSNNNNNN NNNNLGIEGR.

    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.

    Mbp Ecoli His
  • View Data Sheet

    Description:

    ASF1 Anti-Silencing Function 1 Homolog A Human Recombinant

    CGI-98, HSPC146, DKFZp547E2110, ASF1A, Histone chaperone ASF1A, Anti-silencing function protein 1 homolog A, hAsf1, hAsf1a, CCG1-interacting factor A, CIA, hCIA.

    Product # :

    PRO-682

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    Description

    ASF1A Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (1-204 a.a.) and having a molecular mass of 27kDa.ASF1A is fused to a 36 amino acid His Tag and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ASF1A protein solution contains 20mM Tris-HCl, pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      ASF1A is part of the H3/H4 family of histone chaperone proteins corresponding to the anti-silencing function-1 gene in yeast. ASF1A is an important element of the histone donor complex that functions in nucleosome assembly. ASF1A interacts with histones H3 and H4, and functions together with a chromatin assembly factor during DNA replication and repair. Deletion of ASF1A in yeast and Drosophila confers sensitivity to various DNA damaging agents and inhibitors of DNA replication, increases genomic instability and sister chromatid exchange, and activates the DNA damage checkpoint.

    • Synonyms

      CGI-98, HSPC146, DKFZp547E2110, ASF1A, Histone chaperone ASF1A, Anti-silencing function protein 1 homolog A, hAsf1, hAsf1a, CCG1-interacting factor A, CIA, hCIA.

    • 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 KDRWGSMAKV QVNNVVVLDN PSPFYNPFQF EITFECIEDL SEDLEWKIIY VGSAESEEYD QVLDSVLVGP VPAGRHMFVF QADAPNPGLI PDADAVGVTV VLITCTYRGQ EFIRVGYYVN NEYTETELRE NPPVKPDFSK LQRNILASNPRVTRFHINWE DNTEKLEDAE SSNPNLQSLL STDALPSASK GWSTSENSLN VMLESHMDCM.

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    Asf1A Human
  • View Data Sheet

    Description:

    Mannoside Acetylglucosaminyltransferase 2 Human Recombinant, Sf9

    Alpha-1, 6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, MGAT2, CDG2A, CDGS2, GLCNACTII, GNT-II, GNT2, Beta-1,2-N-acetylglucosaminyltransferase II, GlcNAc-T II, Mannoside acetylglucosaminyltransferase 2, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II.

    Product # :

    ENZ-1077

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    Description

    MGAT2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 427 amino acids (30-447a.a.) and having a molecular mass of 49.3kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).MGAT2 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    MGAT2 protein solution (0.25mg/ml) contains 20mM Tris-HCl (pH 7.5), 10% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

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    • Introduction

      MGAT2 is an enzyme which takes part in the catalyzation of a crucial step in the reaction of oligomannose which converts to complex N-glycans. MGAT2 has three domains, classic to glycosyltransferase: short N-terminal cytoplasmic domain, a C-terminal catalytic domain and hydrophobic non-cleavable signal-anchor domain. The enzyme MGAT2 is encoded by the MGAT2 gene in humans. There are no introns in the DNA coding the gene, therefore mutations in the MGAT2 will result in carbohydrate-deficient glycoprotein syndrome, type II.

    • Synonyms

      Alpha-1, 6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase, MGAT2, CDG2A, CDGS2, GLCNACTII, GNT-II, GNT2, Beta-1,2-N-acetylglucosaminyltransferase II, GlcNAc-T II, Mannoside acetylglucosaminyltransferase 2, N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase II.

    • 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

      ADPRQRKNEA LAPPLLDAEP ARGAGGRGGD HPSVAVGIRR VSNVSAASLV PAVPQPEADN LTLRYRSLVY QLNFDQTLRN VDKAGTWAPR ELVLVVQVHN RPEYLRLLLD SLRKAQGIDN VLVIFSHDFW STEINQLIAG VNFCPVLQVF FPFSIQLYPN EFPGSDPRDC PRDLPKNAAL
      KLGCINAEYP DSFGHYREAK FSQTKHHWWW KLHFVWERVK ILRDYAGLIL FLEEDHYLAP DFYHVFKKMW KLKQQECPEC DVLSLGTYSA SRSFYGMADK VDVKTWKSTE HNMGLALTRN AYQKLIECTD TFCTYDDYNW DWTLQYLTVS CLPKFWKVLV PQIPRIFHAG DCGMHHKKTC
      RPSTQSAQIE SLLNNNKQYM FPETLTISEK FTVVAISPPR KNGGWGDIRD HELCKSYRRL QHHHHHH.

    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.

    Mgat2 Protein
  • View Data Sheet

    Description:

    Holo Transferrin Bovine

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

    Product # :

    PRO-510

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    Description

    Bovine Holo Transferrin is a glycoprotein of approximately 80 kDa.

    Formulation

    The protein (1mg/ml) was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by Cellulose Acetate.

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    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered Pink lyophilized (freeze-dried) powder.

    • Stability

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

    • Human Virus Test

      FDA approved Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG, HBc, ALT and Syphilis.Viral inactivation by pasteurization (60°C for 10 hours) has been validated using three different test viruses, with removal of 8-14.5 logs of virus documented. The purification process has also been found to remove significant additional quantities of virus.

    • Applications

      Bovine Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Bovine Transferrin is Critical for long-term cells growth in-vitro. Bovine Transferrin is used as detoxificant in media by binding contaminating metal ions. Bovine Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Bovine Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

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    Holo Transferrin Bovine
  • View Data Sheet

    Description:

    SLAMF1 Human Recombinant

    Signaling lymphocytic activation molecule, CDw150, IPO-3, CD150, SLAMF1, SLAM.

    Product # :

    PRO-1342

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    Description

    SLAMF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (21-237 a.a) and having a molecular mass of 26.7kDa.SLAMF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SLAMF1 protein solution (0.5mg/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

      SLAMF1 is a member of the immunoglobulin gene superfamily and is involved in T-cell stimulation. The SLAMF1 protein is constitutively expressed on peripheral blood memory T cells, T-cell clones, immature thymocytes, and a fraction of B cells, and is swiftly induced on naive T cells after activation. There are probably 2 modes of SLAM signaling: one in which the inhibitor SH2D1A serves as a negative regulator and another in which protein-tyrosine phosphatase 2C (PTPN11)-dependent signal transduction functions.

    • Synonyms

      Signaling lymphocytic activation molecule, CDw150, IPO-3, CD150, SLAMF1, SLAM.

    • 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 MGSASYGTGG RMMNCPKILR QLGSKVLLPL TYERINKSMN KSIHIVVTMA KSLENSVENK IVSLDPSEAG PPRYLGDRYK FYLENLTLGI RESRKEDEGW YLMTLEKNVS VQRFCLQLRL YEQVSTPEIK VLNKTQENGT CTLILGCTVE KGDHVAYSWS EKAGTHPLNP ANSSHLLSLT LGPQHADNIY ICTVSNPISN NSQTFSPWPG CRTDPSETKP.

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    Slamf1 Human
  • View Data Sheet

    Description:

    Neuregulin-1/Heregulin-b1 Human Recombinant

    Neuregulin-1, Heregulin-b1, NRG1-B1, NRG1 B1.

    Product # :

    CYT-733

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    Description

    Recombinant Human Neuregulin-1/Heregulin-b1 produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 177-241) containing 65 amino acids and having a total molecular mass of 7.5kDa. NRG1-B1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in 1×PBS, pH 7.4 and 5% trehalose.

    Purity

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

    Biological Activity

    The ED50 was determined by the dose-dependent stimulation of the proliferation of human MCF-7 cells is less than 0.5ng/ml, corresponding to a specific activity of >2.0×106 units/mg.

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    • Introduction

      Neuregulin/Heregulin is a family of structurally related polypeptide growth factors which are stemmed from alternatively spliced genes (NRG1, NRG2, NRG3 and NRG4). Thus far, there are more than 14 soluble and transmembrane proteins derived from the NRG1 gene. Proteolytic processing of the extracellular domain of the transmembrane NRG1 isoforms release soluble growth factors. HRG1-b1 is comprised of an Ig domain and an EGF-like domain which is necessary for direct binding to receptor tyrosine kinases erb3 and erb4. This binding stimulates erb3 and erb4 heterodimerization with erb2, promoting intrinsic kinase activity, which results in tyrosine phosphorylation. Even though HRG1-b1 biological effects are still unclear, it has been discovered to advance motility and invasiveness of breast cancer cells which in addition might entail up-regulation of expression and function of the autocrine motility-promoting factor (AMF).

    • Synonyms

      Neuregulin-1, Heregulin-b1, NRG1-B1, NRG1 B1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NRG1-B1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NRG1-B1 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 NRG1-B1 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SHLVKCAEKE KTFCVNGGEC FMVKDLSNPS RYLCKCPNEF TGDRCQNYVM ASFYKHLGIE FMEAE.

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    Nrg1 B1 Human
  • View Data Sheet

    Description:

    V-crk Sarcoma Virus CT10 Oncogene Human Recombinant

    Adapter molecule crk, Proto-oncogene c-Crk, p38, CRK, CRKII.

    Product # :

    PRO-275

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    Description

    CRK Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 224 amino acids (1-204 a.a.) and having a molecular mass of 25kDa. The CRK is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRK solution (0.5 mg/ml) contains 20mM Tris-HCl Buffer (pH 8.0) and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      CRK belongs to the signaling adapter protein family which binds to several tyrosine-phosphorylated proteins. CRK is involved in many cellular processes such as apoptosis, proliferation, and differentiation. CRK has a modular domain architecture consisting of an SH2 followed by two SH3 domains (src-homology domains). The N-terminal SH2 domain of the CRK protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation.

    • Synonyms

      Adapter molecule crk, Proto-oncogene c-Crk, p38, CRK, CRKII.

    • 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).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAGNFDSEER SSWYWGRLSR QEAVALLQGQ RHGVFLVRDS STSPGDYVLS VSENSRVSHY IINSSGPRPP VPPSPAQPPP GVSPSRLRIG DQEFDSLPAL LEFYKIHYLD TTTLIEPVSR SRQGSGVILR QEEAEYVRAL FDFNGNDEED LPFKKGDILR IRDKPEEQWW NAEDSEGKRG MIPVPYVEKY RPASASVSAL IGGR.

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    CRK Human
  • View Data Sheet

    Description:

    V-Set and Transmembrane Domain Containing 2 Like Human Recombinant

    V-set and transmembrane domain-containing protein 2-like protein, VSTM2L, C20orf102, dJ1118M15.2.

    Product # :

    PRO-1018

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    Description

    VSTM2L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (25-204 a.a.) and having a molecular mass of 22.6kDa. VSTM2L is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    VSTM2L protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl,1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      V-set and transmembrane domain containing 2 (VSTM2L) is a novel modulator of HN neuroprotective activity. VSTM2L colocalizes with HN in distinct brain areas as well as in primary cultured neurons, where it plays a part in the modulation of neuronal viability. When tested in HN neuroprotection bioassays, VSTM2L acts as a potent antagonist of HN neuroprotective activity. The VSTM2L protein is the first example of a secreted antagonist of HN and may have a role in the modulation of HN biological functions.

    • Synonyms

      V-set and transmembrane domain-containing protein 2-like protein, VSTM2L, C20orf102, dJ1118M15.2.

    • 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 MGSHMTRPAG HAPWDNHVSG HALFTETPHD MTARTGEDVE MACSFRGSGS PSYSLEIQWW YVRSHRDWTD KQAWASNQLK ASQQEDAGKE ATKISVVKVV GSNISHKLRL SRVKPTDEGS YECRVIDFSD GKARHHKVKA YLRVQPGENS VLHLPEAPPA APAPPPPKPG KELRKRSVDQ EACSL.

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    Vstm2L Human
  • View Data Sheet

    Description:

    Fibroblast Growth Factor-18 Human Recombinant, His Tag

    Fibroblast growth factor 18, FGF-18, zFGF5, FGF18.

    Product # :

    CYT-935

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    Description

    FGF18 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (Glu28-Ala207) containing 190 amino acids including a 10 aa His tag at N-terminus. The total calculated molecular mass is 22.3kDa.

    Source

    Escherichia Coli.

    Formulation

    FGF18 was filtered (0.4µm) and lyophilized in phosphate buffered saline and 5% w/v trehalose.

    Purity

    Purity as determined by densitometric image analysis is greater than 95%.

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    • Introduction

      Fibroblast growth factor 18 (FGF18) is a member of the large FGF family which has at least 23 members. FGF18 is a binding growth factor with a core 120 amino acid FGF domain which allows for a common tertiary structure. FGFs are expressed in the course of the embryonic development and in restricted adult tissues. FGF-18 is an indispensable regulator of long bone and calvarial development. FGF-18 signals via FGFR 1c, 2c, 3c, and 4.

    • Synonyms

      Fibroblast growth factor 18, FGF-18, zFGF5, FGF18.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. FGF18 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASEENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQPELQK PFKYTTVTKR SRRIRPTHPA.

    • Background

      What is the molecular weight/Mw of FGF18 HIS Protein?
      FGF18 HIS Protein has a total Mw of 22.3kDa.

      What is the source or expression system of FGF18 HIS Protein?
      Escherichia Coli.

      What is the Purity of FGF18 HIS Protein?
      FGF18 HIS Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of FGF18 HIS Protein?
      The biological functionality of FGF18 HIS Protein will be determined in the future.

      What is the amino acid sequence of FGF18 HIS Protein?
      MKHHHHHHASEENVDFRIHV ENQTRARDDV SRKQLRLYQL YSRTSGKHIQ VLGRRISARG EDGDKYAQLL VETDTFGSQV RIKGKETEFY LCMNRKGKLV GKPDGTSKEC VFIEKVLENN YTALMSAKYS GWYVGFTKKG RPRKGPKTRE NQQDVHFMKR YPKGQPELQK PFKYTTVTKR SRRIRPTHPA.

      What applications can FGF18 HIS Protein be used in?
      FGF18 HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FGF18 HIS Protein?
      The endotoxin level is minimal, FGF18 HIS Protein was purified using conventional chromatography techniques.

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    Fgf 18 Human His