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  • Cytokines
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  • Tumor Necrosis Factor

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    B-Cell Activating Factor

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  • Beta Defensin

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  • Bone Morphogenetic Protein

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  • B type Natriuretic Peptide

    B type Natriuretic Peptide

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  • BST

    BST

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    Betacellulin

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    Insulin-Like Growth Factor

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    C-10 (CCL6)

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  • Other Chemokines

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  • MEC (CCL28)

    MEC (CCL28)

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  • LD78-beta (CCL3L1)

    LD78-beta (CCL3L1)

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  • CTACK (CCL27)

    CTACK (CCL27)

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  • CXCL16

    CXCL16

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    CXCL17

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    Platelet Factor-4 (CXCL4)

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  • ENA-78 (CXCL5)

    ENA-78 (CXCL5)

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  • Eotaxin (CCL11,24,26)

    Eotaxin (CCL11,24,26)

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  • Actin

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  • Ankyrin Repeat Domain

    Ankyrin Repeat Domain

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  • Annexin

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  • Aprotinin

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Search results

1000 results found for “calcyphosine”

Name

Description

Product #

Price

Quantity

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  • View Data Sheet

    Name :

    SOST Mouse

    Description:

    Sclerostin Mouse Recombinant

    SOST, Sclerostin, 5430411E23Rik.

    Product # :

    PRO-2670

    Price :

    Quantity :

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    Description

    SOST Mouse Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (24-211 a.a) containing 194 amino acids and having a molecular mass of 21.9 kDa.SOST is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293 cells.

    Formulation

    SOST protein (0.25mg/ml) contains 10% glycerol and Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is expressed mainly in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.

    • Synonyms

      SOST, Sclerostin, 5430411E23Rik.

    • 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

      QGWQAFRNDA TEVIPGLGEY PEPPPENNQT MNRAENGGRP PHHPYDAKDV SEYSCRELHY TRFLTDGPCR SAKPVTELVC SGQCGPARLL PNAIGRVKWW RPNGPDFRCI PDRYRAQRVQ LLCPGGAAPR SRKVRLVASC KCKRLTRFHN QSELKDFGPE TARPQKGRKP RPGARGAKAN QAELENAYHH HHHH

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Sclerostin Mouse
  • View Data Sheet

    Name :

    Polcalcin Phl p 7

    Description:

    Pollen Allergen Phl p 7 Recombinant

    Polcalcin Phl p 7, Calcium-binding pollen allergen Phl p 7, P7, Phl p 7.

    Product # :

    ALR-015

    Price :

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    Description

    Recombinant Polcalcin Phl p 7 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 9.0 kDa. Polcalcin Phl p 7 is purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Polcalcin Phl p 7 is supplied in 20mM HEPES buffer pH-8.0, 0.2M NaCl, 1mM CaCl2 and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Phl p 7.0101 is a secondary allergen of timothy grass pollen, which is non-glycosylated protein. Grass pollen-sensitized individuals show IgE antibodies in their blood system. Phl p 7.0101 is a calcium binding protein with similar sequence to pollen antigens that exist in different plants, hence, cross-reactions are possible.

    • Synonyms

      Polcalcin Phl p 7, Calcium-binding pollen allergen Phl p 7, P7, Phl p 7.

    • 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    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.

    Polcalcin Phl P 7
  • View Data Sheet

    Name :

    S100A6 Human

    Description:

    S100 Calcium Binding Protein A6 Human Recombinant

    Protein S100-A6, Calcyclin, Growth factor-inducible protein 2A9, MLN 4, Prolactin receptor-associated protein, PRA, S100 calcium-binding protein A6, S100A6, CACY, 2A9, 5B10, CABP.

    Product # :

    PRO-148

    Price :

    Quantity :

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    Description

    S100A6 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 110 amino acids (1-90 a.a.) and having a molecular mass of 12.3kDa. The S100A6 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The S100A6 solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 30% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100A6 is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized either in the cytoplasm or the nucleus of a wide range of cells. S100 proteins are involved in the regulation of a number of cellular processes such as cell cycle progression and differentiation. There are at least 13 members in the S100 gene family, which are located as a cluster on chromosome 1q21. S100A6 function in stimulation of prolactin secretion and exocytosis. Chromosomal rearrangements and altered expression of the S100A6 gene are implicated in melanoma.

    • Synonyms

      Protein S100-A6, Calcyclin, Growth factor-inducible protein 2A9, MLN 4, Prolactin receptor-associated protein, PRA, S100 calcium-binding protein A6, S100A6, CACY, 2A9, 5B10, CABP.

    • 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 MACPLDQAIG LLVAIFHKYS GREGDKHTLS KKELKELIQK ELTIGSKLQD AEIARLMEDL DRNKDQEVNF QEYVTFLGAL ALIYNEALKG.

    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.

    S100A6 Human
  • View Data Sheet

    Name :

    CXADR Human

    Description:

    Coxsackie Virus And Adenovirus Receptor Human Recombinant

    Coxsackie Virus And Adenovirus Receptor, CAR, 46 KD Coxsackievirus And Adenovirus Receptor (CAR) Protein 11, Coxsackievirus B-Adenovirus Receptor, HCVADR, CVB3-Binding Protein, CAR4/6, HCAR.

    Product # :

    PRO-1548

    Price :

    Quantity :

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    Description

    CXADR Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 241 amino acids (20-237) and having a molecular mass of 26.0kDa.CXADR is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CXADR solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      CXADR is a component of the epithelial apical junction complex which operates as an homophilic cell adhesion molecule and is crucial for tight junction integrity. CXADR also takes part in transepithelial relocation of leukocytes through adhesive interactions with AMICA1/JAML a transmembrane protein of the plasma membrane of leukocytes. A number of transcript variants encoding different isoforms were identified for this gene. Pseudogenes of this gene were located on chromosomes 15, 18, and 21.

    • Synonyms

      Coxsackie Virus And Adenovirus Receptor, CAR, 46 KD Coxsackievirus And Adenovirus Receptor (CAR) Protein 11, Coxsackievirus B-Adenovirus Receptor, HCVADR, CVB3-Binding Protein, CAR4/6, HCAR.

    • 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 MGSLSITTPE EMIEKAKGET AYLPCKFTLS PEDQGPLDIE WLISPADNQK VDQVIILYSG DKIYDDYYPD LKGRVHFTSN DLKSGDASIN VTNLQLSDIG TYQCKVKKAP GVANKKIHLV VLVKPSGARC YVDGSEEIGS DFKIKCEPKE GSLPLQYEWQ KLSDSQKMPT SWLAEMTSSV ISVKNASSEY SGTYSCTVRN RVGSDQCLLR LNVVPPSNKA G.

    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.

    Cxadr Human
  • View Data Sheet

    Name :

    CLCF1 Human, His

    Description:

    Neurotrophin-1 Human Recombinant, His Tag

    Cardiotrophin-like cytokine factor 1, B-cell-stimulating factor 3, BSF-3, Novel neurotrophin-1, NNT-1, CLCF1, BSF3, CLC, NNT1, NR6, CISS2.

    Product # :

    CYT-071

    Price :

    Quantity :

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    • sds-page

    Description

    CLCF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 219 amino acids (28-225 a.a) and having a molecular mass of 24.6kDa.CLCF1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CLCF1 protein solution (1mg/ml) containing 20mM sodium citrate (pH 3.5), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    sds-page

    CLCF-sds-page - Product image 1

    More Info

    • Introduction

      Cardiotrophin-like cytokine factor 1 (CLCF1) is a member of the interleukin 6 family of cytokines, which are involved in cell signaling via phosphorylation of gp130. CLCF1 has a sequence of 225 amino acids with a 27 aa signal peptide, having a molecular mass of 22kDa in the mature form, and the maximum homology to cardiotrophin-1 and ciliary neurotrophic factor. CLCF1 is actively secreted from cells by forming a complex with soluble type I CRLF1 or soluble CNTFR. Defects in the CLCF1 gene cause cold-induced sweating syndrome 2 (CISS2). The CISS2 syndrome is typified by profuse sweating after exposure to cold as well as congenital physical abnormalities of the head and spine.

    • Synonyms

      Cardiotrophin-like cytokine factor 1, B-cell-stimulating factor 3, BSF-3, Novel neurotrophin-1, NNT-1, CLCF1, BSF3, CLC, NNT1, NR6, CISS2.

    • 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 MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.

    • Background

      Cardiotrophin-Like Cytokine Factor 1 Human Recombinant: A Significant Player in Neuronal Development and Immune Regulation

      Cardiotrophin-like cytokine factor 1 (CLCF1) has emerged as a crucial player in neuronal development and immune regulation. As a heterodimeric neurotropic cytokine, CLCF1 in complex with cytokine-like factor-1 (CLF-1) has demonstrated vital roles in neuronal development. Studies show that mice lacking this heterodimer exhibit reduced motor neurons and die shortly after birth due to suckling defects. In humans, mutations in the genes encoding for CLCF1 and CLF-1 manifest as Sohar-Crisponi or cold-induced sweating syndrome, with individuals at high risk of early death​1​.

      CLCF1 also exhibits a significant role in the regulation of hematopoiesis, particularly skewing towards myeloid cell differentiation. It has been demonstrated that in mice, CLCF1 promotes B-cell expansion, enhances humoral responses, and triggers autoimmunity. Further, CLCF1 administration resulted in an increase in circulating myeloid cells, along with augmented hematopoietic progenitor cells in the bone marrow. These findings underscore CLCF1's crucial role in modulating the immune system, particularly in the context of bonemarrow transplants and recovery following sub-lethal irradiation​2​.

      Interestingly, CLCF1 is a member of the IL-6 family of cytokines, known for their significant roles in immune regulation and stem cell biology. Like other family members, CLCF1 is secreted as a composite cytokine with CRLF1 and signals through the heterodimerization of the signaling chains LIFRβ and gp130. This suggests overlapping functions with leukemia inhibitor factor (LIF), another IL-6 family member. Expression of CLCF1 is documented in lymph nodes, spleen, and circulating lymphocytes, further establishing its role in immune modulation. However, the comprehensive implications of CLCF1 in immune regulation and hematopoiesis remain an active area of investigation​3​.

      In summary, Cardiotrophin-like cytokine factor 1 human recombinant represents a promising area of research with potential therapeutic implications in neurodevelopmental disorders and immune regulation.

      What is the molecular weight/Mw of CLCF Protein?
      CLCF Protein has a total Mw of 24.6kDa.

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

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

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

      What is the amino acid sequence of CLCF Protein?
      MGSSHHHHHH SSGLVPRGSH MLNRTGDPGP GPSIQKTYDL TRYLEHQLRS LAGTYLNYLG PPFNEPDFNP PRLGAETLPR ATVDLEVWRS LNDKLRLTQN YEAYSHLLCY LRGLNRQAAT AELRRSLAHF CTSLQGLLGS IAGVMAALGY PLPQPLPGTE PTWTPGPAHS DFLQKMDDFW LLKELQTWLW RSAKDFNRLK KKMQPPAAAV TLHLGAHGF.

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

      What is the endotoxin level for CLCF Protein?
      The endotoxin level is minimal, CLCF Protein was purified using conventional chromatography techniqu

    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.

    Clcf1 Human
  • View Data Sheet

    Name :

    VAMP8 Human

    Description:

    Endobrevin Human Recombinant

    VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.

    Product # :

    PRO-660

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    Description

    VAMP8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 96 amino acids (1-76 a.a.) and having a molecular mass of 10.9 kDa. The VAMP8 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The VAMP8 protein solution (0.25mg/ml) contains 20mM Tris pH-8, 0.1mM PMSF, 0.2M NaCl and 50% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      VAMP8 also called endobrevin, is the main component of a SNARE complex involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. VAMP8 protein is involved in the regulatation of enzyme secretion in pancreatic acinar cells and plays a part in the abscission of the midbody during cell division, which leads to completely separate daughter cells. VAMP8 is essential for dense-granule secretion in platelets. VAMP8 is related with the perinuclear vesicular structures of the early endocytic compartment. VAMP8 interacts particularly with the soluble NSF-attachment protein (alpha-SNAP), through an VAMP8-containing SNARE complex.

    • Synonyms

      VAMP8, VAMP-8, Endobrevin, Vesicle-Associated Membrane Protein 8, EDB.

    • 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 MEEASEGGGN DRVRNLQSEV EGVKNIMTQN VERILARGEN LEHLRNKTED LEATSEHFKT TSQKVARKFW WKNVKM.

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    Vamp8 Human
  • View Data Sheet

    Name :

    Thymosin a1 human

    Description:

    Thymosin a1 Acetate

    Product # :

    HOR-243

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    Description

    Thymosin a1 acetate, also known as thymalfasin has immunoregulatory properties enhancing immune functions. Thymosin a1 has a molecular formula of C129H215N33O55 a.a. sequence of Ac-Ser-Asp-Ala-Ala-Val-Asp-Thr-Ser-Ser-Glu-Ile-Thr-Thr-Lys-Asp-Leu-Lys-Glu-Lys-Lys-Glu-Val-Val-Glu-Glu-Ala-Glu-Asn-OH and having a Mw of 3108.32 Dalton.

    Formulation

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

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Thymalfasin is a synthetic analogue of thymosin-alpha-1, a 28-amino acid protein derived from the precursor protein prothymosin-alpha. Exhibiting a variety of immunoregulating properties, thymosin-alpha-1 induces differentiation of murine T-cell precursors and human thymocytes and the terminal differentiation of functionally immature cord blood lymphocytes and induces production of IL-2, high affinity IL-2 receptors, and B-cell growth factors by peripheral blood mononuclear cells. T-helper and cytotoxic/suppressor T-cell populations are targets of thymosin activity. Thymosin-alpha-1 has been shown to increase the efficiency of antigen presentation by macrophages and to be an endogenous modulator of alpha-thrombin activity.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Thymosin a1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymalfasin 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 Thymosin a1 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      What is the molecular weight/Mw of THYMOSIN-A1 HUMAN Protein?
      THYMOSIN-A1 HUMAN Protein has a total Mw of 3.1kDa.

      What is the Purity of THYMOSIN-A1 HUMAN Protein?
      THYMOSIN-A1 HUMAN Protein is >99% pure as determined by SDS-PAGE.

      What is the Biological Activity of THYMOSIN-A1 HUMAN Protein?
      The biological functionality of THYMOSIN-A1 HUMAN Protein will be determined in the future.

      What applications can THYMOSIN-A1 HUMAN Protein be used in?
      THYMOSIN-A1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for THYMOSIN-A1 HUMAN Protein?
      The endotoxin level is minimal, THYMOSIN-A1 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.

    Thymosin Alpha 1
  • View Data Sheet

    Name :

    CNTF Human

    Description:

    Ciliary-Neurotrophic Factor Human Recombinant

    HCNTF, CNTF, Ciliary Neurotrophic Factor.

    Product # :

    CYT-272

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    Description

    Ciliary Neurotrophic Factor Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 22706 Dalton. The CNTF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 5mM sodium Phosphate buffer pH=7.5 and 5mM sodium chloride.

    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 TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

    More Info

    • Introduction

      CNTF is a polypeptide hormone whose actions appear to be restricted to the nervous system where it promotes neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. The protein is a potent survival factor for neurons and oligodendrocytes and may be relevant in reducing tissue destruction during inflammatory attacks. A mutation in this gene, which results in aberrant splicing, leads to ciliary neurotrophic factor deficiency, but this phenotype is not causally related to neurologic disease. In addition to the predominant monocistronic transcript originating from this locus, the gene is also co-transcribed with the upstream ZFP91 gene. Co-transcription from the two loci results in a transcript that contains a complete coding region for the zinc finger protein but lacks a complete coding region for ciliary neurotrophic factor.
      CNTF is a survival factor for various neuronal cell types. Seems to prevent the degeneration of motor axons after axotomy.

    • Synonyms

      HCNTF, CNTF, Ciliary Neurotrophic Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Ciliary Neurotrophic Factor although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CNTF 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 HCNTF 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 five N-terminal amino acids was determined and was found to be Met-Ala-Phe-Thr-Glu.

    • Background

      Exploring the Potential of Human Recombinant Ciliary-Neurotrophic Factor: Implications and Applications

      Abstract:

      Ciliary-Neurotrophic Factor (CNTF) holds remarkable promise in neurobiology and therapeutic development due to its neuroprotective and regenerative properties. This paper delves into the significance of Human Recombinant CNTF, its production methodologies, and its potential applications in treating neurodegenerative disorders. The review sheds light on the therapeutic potential of CNTF and its role in advancing neuroregeneration research.

      Introduction:

      CNTF, a neurotrophic cytokine, is known for its pivotal role in neuronal survival and growth. The availability of Human Recombinant CNTF allows researchers to investigate its therapeutic potential and explore avenues for developing novel treatments for neurodegenerative diseases. CNTF's ability to support neuronal health and promote regeneration makes it a promising candidate for medical interventions.

      Mechanisms of Action:

      CNTF interacts with specific receptor complexes, activating various downstream signaling pathways, including Janus kinase (JAK) and Signal Transducer and Activator of Transcription (STAT) pathways. These pathways contribute to cell survival, differentiation, and axonal growth, forming the foundation for CNTF's neuroprotective effects.

      Production Methods:

      Human Recombinant CNTF is produced by introducing the CNTF gene into suitable expression systems, often employing bacterial or mammalian cells. Ensuring proper post-translational modifications is essential for maintaining the protein's biological activity and therapeutic potential.

      Therapeutic Applications:

      CNTF's neuroprotective and regenerative effects offer potential therapeutic applications in neurodegenerative disorders, such as amyotrophic lateral sclerosis (ALS), retinal degeneration, and Parkinson's disease. It holds promise for preserving and restoring neuronal function, thereby improving the quality of life for affected individuals.

      Challenges and Future Directions:

      While Human Recombinant CNTF shows great potential, challenges include precise dosing, delivery methods, and potential side effects. Further research is needed to optimize CNTF-based therapies and assess their long-term safety and efficacy in clinical settings.

      Conclusion:

      Human Recombinant Ciliary-Neurotrophic Factor emerges as a critical tool in advancing our understanding of neuroprotection and neuroregeneration. Its potential in treating neurodegenerative disorders highlights the ongoing quest for innovative therapeutic approaches that harness the body's inherent ability to heal and regenerate.

      What is the molecular weight/Mw of CNTF Protein?
      CNTF Protein has a total Mw of 22kDa.

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

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

      What is the Biological Activity of CNTF Protein?
      The ED50 as determined by the dose-dependant stimulation of TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.

      What is the amino acid sequence of CNTF Protein?
      CNTF Protein is composed from 199 amino acids.

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

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

    • Protein content

      CNTF quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 1.28 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 CNTF Recombinant 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.

    Cntf Human
  • View Data Sheet

    Name :

    Activin A Human Plant

    Description:

    Activin A Human Recombinant, Plant

    Inhba, Inhibin beta A, FSH releasing protein.

    Product # :

    CYT-052

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    Description

    Activin A human Recombinant produced in Nicotiana benthamiana plant is a disulfide-linked homodimers of two betaA chains, each containing 116 amino residues (molecular formula C600H911N173O174S13) and 6-His-tag at the N-terminal having the total molecular mass of 27.4kDa.

    Source

    Nicotiana benthamiana plant

    Formulation

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

    Purity

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

    More Info

    • Introduction

      Activins are homodimers or heterodimers of the different ? subunit isoforms, part of the TGF? family. Mature Activin A has two 116 amino acids residues betaA subunits (bA-bA). 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

      Sterile Filtered White 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

      It is recommended to reconstitute the lyophilized Activin A in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS

    • 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?
      Nicotinia

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

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

      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?
      HHHHHHGLEC DGKVNICCKK QFFVSFKDIG WNDWIIAPSG YHANYCEGEC PSHIAGTSGS SLSFHSTVIN HYRMRGHSPF ANLKSCCVPT KLRPMSMLYY DDGQNIIKKD IQNMIVEECG CS

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

    • Serological Identification

      The protein was electrophoresed under reducing condition on a 15% SDS-polyacrylamide gel, transferred by electroblotting to a NC membrane and visualized by immune-detection with specific antibody Activin A.

    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 Human Plant
  • View Data Sheet

    Name :

    CAMK4 Human

    Description:

    Calcium/Calmodulin-Dependent Protein Kinase IV Human Recombinant

    Calcium/calmodulin-dependent protein kinase type IV catalytic chain, CaMK-GR, CaM kinase-GR, CaMK IV, IV, brain Ca(2+)-calmodulin-dependent protein kinase type IV, caMK, CAM kinase IV, EC 2.7.11.17.

    Product # :

    PKA-021

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    Description

    CAMK4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 497 amino acids (1-473) and having a molecular mass of 54.5kDa.CAMK4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The CAMK4 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      CAMK4 is a member of the serine/threonine protein kinase family, and of the Ca(2+)/calmodulin-dependent protein kinase subfamily. CAMK4 is a multifunctional serine/threonine protein kinase with restricted tissue distribution which is associated to transcriptional regulation in lymphocytes, neurons and male germ cells.

    • Synonyms

      Calcium/calmodulin-dependent protein kinase type IV catalytic chain, CaMK-GR, CaM kinase-GR, CaMK IV, IV, brain Ca(2+)-calmodulin-dependent protein kinase type IV, caMK, CAM kinase IV, EC 2.7.11.17.

    • 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 MGSHMLKVTV PSCSASSCSS VTASAAPGTA SLVPDYWIDG SNRDALSDFF EVESELGRGA TSIVYRCKQK GTQKPYALKV LKKTVDKKIV RTEIGVLLRL SHPNIIKLKE IFETPTEISL VLELVTGGEL FDRIVEKGYY SERDAADAVK QILEAVAYLH ENGIVHRDLK PENLLYATPA PDAPLKIADF GLSKIVEHQV LMKTVCGTPG YCAPEILRGC AYGPEVDMWS VGIITYILLC GFEPFYDERG DQFMFRRILN CEYYFISPWW DEVSLNAKDL VRKLIVLDPK KRLTTFQALQ HPWVTGKAAN FVHMDTAQKK LQEFNARRKL KAAVKAVVAS SRLGSASSSH GSIQESHKAS RDPSPIQDGN EDMKAIPEGE KIQGDGAQAA VKGAQAELMK VQALEKVKGA DINAEEAPKM VPKAVEDGIK VADLELEEGL AEEKLKTVEE AAAPREGQGS SAVGFEVPQQ DVILPEY.

    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.

    Camk4 Human
  • View Data Sheet

    Name :

    PPIH Human, His

    Description:

    Cyclophilin-H Human Recombinant, His Tag

    Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.

    Product # :

    ENZ-730

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    Description

    PPIH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 2-177) containing 186 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 20.3kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4 µm) and lyophilized from 0.5 mg/ml in phosphate buffered saline pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PPIH is a part of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and increase protein folding. PPIH enzyme is a precise factor of the complex that comprises pre-mRNA processing factors PRPF3, PRPF4, and PRPF18, as well as U4/U5/U6 tri-snRNP. PPIH possess PPIase activity and acts as a protein chaperone that mediates the interactions between different proteins inside the spliceosome.

    • Synonyms

      Oeptidylprolyl Isomerase H, PPIH, CYPH, CYP20, SnuCyp-20, Peptidyl-prolyl cis-trans isomerase H, PPIase H, Rotamase H, U-snRNP-associated cyclophilin SnuCyp-20, USA-CYP, Small nuclear ribonucleoprotein particle-specific cyclophilin H, peptidylprolyl isomerase H, CYP-20, MGC5016, Cyclophilin-H.

    • 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. PPIH is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASAVANSSPVNP VVFFDVSIGG QEVGRMKIEL FADVVPKTAE NFRQFCTGEF RKDGVPIGYK GSTFHRVIKD FMIQGGDFVN GDGTGVASIY RGPFADENFK LRHSAPGLLS MANSGPSTNG CQFFITCSKC DWLDGKHVVF GKIIDGLLVM RKIENVPTGP NNKPKLPVVI SQCGEM.

    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.

    Ppih Human His
  • View Data Sheet

    Name :

    CDHR5 Mouse

    Description:

    Cadherin Related Family Member 5 Mouse Recombinant

    Cadherin-related family member 5, Mu-protocadherin, Cdhr5, Mucdhl, Mupcdh, 1810074H01Rik, AI481143

    Product # :

    PRO-2647

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    Description

    CDHR5 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 621 amino acids (29-641 a.a) and having a molecular mass of 66.3kDa.CDHR5 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The CDHR5 solution (0.25mg/1ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CDHR5, also referred to ascadherin-related family member 5, is a calcium-dependent cell adhesion protein. CDHR5 is located in coated pits, and is expressed during lung and kidney developmentat at the lateral and basal surfaces of epithelia.

    • Synonyms

      Cadherin-related family member 5, Mu-protocadherin, Cdhr5, Mucdhl, Mupcdh, 1810074H01Rik, AI481143

    • 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

      QTQVCSVNQT IFRVEENTTV SEPLVNIFVP DGLHVTLGPL STPYAFRIEG KDLFLNVTPD YEENSLLQAD VECKRGDAVV VRLEVFVAVL DINDNAPKFS FEIKTFNVSE DTKVNTTVIP ETQLKATDAD INDILVYTLQ EVTPNASKFF SLEGVNYPAL KLDQTLDYFK NQNMTFMLLA RDTWEENVEP SHTATATLVL NTLPADLRTP WFLPCSFTDG YVCIHAQYSA VVPTGHKLPS PLIMSPGPIY AVDGDQAINQ SIIYSIIAGN TDGTFIINAH DGNLTMTKSI PSPMKFTLLI RADQEDMAQY SVTQAIVEAR SVTGNPLQFS QSLYYGTVVL GSEAGTAVKD KTFPSEILRI QAQYPGFPDL NSAVTYRVTN SSEFMMNKDI MLTAVPMEEA RTIRVEVEAS NTVTKDTATA VVEIQVSERE LPSTEFPTPP EAGGTTGPSS NTTMEAPLTS GTSQRPATTS SGGSVGPFPP GGTTLRPPTP ASSIPGGSPT LGTSTSPQTT TPGGDSAQTP KPGTSHPTAP TSRTSTSLMT TSSRSDSTQT PKPGTSQPMV PIPGASTSSQ PATPSGSSPQ TPKPGTSQST ATGPISGAGE QGDGQRFSTV DMALEHHHHH 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.

    Cdhr5 Mouse
  • View Data Sheet

    Name :

    CTACK Mouse

    Description:

    CTACK Mouse Recombinant (CCL27)

    C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.

    Product # :

    CHM-013

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    Description

    CTACK Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 95 amino acids and having a molecular mass of 10.9kDa. The CTACK is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in 20mM PB, pH7.4 and 300mM 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 lymphocytes is in a concentration range of 10-100 ng/ml.

    More Info

    • Introduction

      CTACK is a chemotactic factor that attracts skin-associated memory T-lymphocytes. CTACK is involved in mediating homing of lymphocytes to cutaneous sites. CTACK Binds to CCR10.

    • Synonyms

      C-C motif chemokine 27, CC chemokine ILC, Cutaneous T-cell-attracting chemokine, CTACK, ESkine, IL-11 R-alpha-locus chemokine, ALP, mILC, Skinkine, Small-inducible cytokine A27, Ccl27, Ilc, Scya27.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.

    • Background

      What is the molecular weight/Mw of CTACK MOUSE Protein?
      CTACK MOUSE Protein has a total Mw of 10.9kDa.

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

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

      What is the Biological Activity of CTACK MOUSE Protein?
      The biological activity determined by a chemotaxis bioassay using human peripheral blood lymphocytes is in a concentration range of 10-100 ng/ml.

      What is the amino acid sequence of CTACK MOUSE Protein?
      LPLPSSTSCC TQLYRQPLPS RLLRRIVHME LQEADGDCHL QAVVLHLARR SVCVHPQNRS LARWLERQGK RLQGTVPSLN LVLQKKMYSN PQQQN.

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

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

    Ctack Mouse
  • View Data Sheet

    Name :

    CCL3L1 Human, His

    Description:

    LD78-beta (CCL3L1) Human Recombinant, His Tag

    C-C motif chemokine 3-like 1, G0/G1 switch regulatory protein 19-2, LD78-beta(1-70), PAT 464.2, Small-inducible cytokine A3-like 1, Tonsillar lymphocyte LD78 beta protein, CCL3L1, D17S1718, G0S19-2, SCYA3L1, LD78, 464.2, SCYA3L, LD78BETA, MGC12815.

    Product # :

    CHM-251

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    Description

    CCL3L1 Human Recombinant fused with a 22 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 90 amino acids (26-93 a.a.) and having a molecular mass of 10kDa. The CCL3L1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL3L1 solution (0.25 mg/ml) contains Phosphate Buffered Saline pH7.4 containing 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCL3L1 is a small cytokine that belongs to the CC chemokines. The CCL3L1 gene is one of several cytokine genes clustered on the q-arm of chromosome 17. CCL3L1 is involved in immunoregulatory and inflammatory processes. CCL3L1 binds to several chemokine receptors including CCBP2 and CCR5. CCR5 is a co-receptor for HIV, and binding of the CCL3L1 protein to CCR5 inhibits HIV entry.

    • Synonyms

      C-C motif chemokine 3-like 1, G0/G1 switch regulatory protein 19-2, LD78-beta(1-70), PAT 464.2, Small-inducible cytokine A3-like 1, Tonsillar lymphocyte LD78 beta protein, CCL3L1, D17S1718, G0S19-2, SCYA3L1, LD78, 464.2, SCYA3L, LD78BETA, MGC12815.

    • 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 MSLAADTPTA CCFSYTSRQI PQNFIADYFE TSSQCSKPSV IFLTKRGRQV CADPSEEWVQ KYVSDLELSA.

    • Background

      What is the molecular weight/Mw of CCL3L1 HUMAN, HIS Protein?
      CCL3L1 HUMAN, HIS Protein has a total Mw of 10kDa.

      What is the source or expression system of CCL3L1 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL3L1 HUMAN, HIS Protein?
      CCL3L1 HUMAN, HIS Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL3L1 HUMAN, HIS Protein?
      The biological functionality of CCL3L1 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL3L1 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MSLAADTPTA CCFSYTSRQI PQNFIADYFE TSSQCSKPSV IFLTKRGRQV CADPSEEWVQ KYVSDLELSA.

      What applications can CCL3L1 HUMAN, HIS Protein be used in?
      CCL3L1 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL3L1 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL3L1 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.

    Ccl3L1 Human His
  • View Data Sheet

    Name :

    VAMP3 Human

    Description:

    Synaptobrevin-3 Human Recombinant

    VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.

    Product # :

    PRO-652

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    Description

    VAMP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The VAMP3 protein solution contains 20mM Tris pH-7.5 and 10% glycerol.

    Purity

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

    More Info

    • Introduction

      VAMP3 is present in recycling endosomes and endosome-derived vesicles. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. VAMP-3 is present in human platelets and necessary for granule secretion. Synaptobrevins are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP3 high homology to other VAMPs in its broad tissue distribution and subcellular localization is shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.

    • Synonyms

      VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.

    • 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

      MSTGPTAATG SNRRLQQTQN QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF ETSAAKLKRK YWWKNCK.

    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.

    Vamp3 Human
  • View Data Sheet

    Name :

    CTSD Human

    Description:

    Cathepsin-D Human Recombinant

    Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.

    Product # :

    ENZ-378

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    Description

    CTSD produced in HEK293 cells is a single, glycosylated polypeptide chain containing 398 amino acids (21-412 a.a.) and having a molecular mass of 43.4kDa. CTSD is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 Cells

    Formulation

    CTSD at 1mg/ml in 50mM MES, pH5.5, 100mM NaCl and 20% Glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE

    More Info

    • Introduction

      Cathepsin D is synthesized as a 54kDa precursor, which is proteolytically processed to an intermediate 48kDa single chain, which matures into more stable 34kDa and 14kDa two chain form. It is an estrogen-regulated lysosomal protease that has been suggested to facilitate cancer cell migration and invasion by digesting the basement membrane, extracellular matrix, and xonnective tissue. Because of its mitogenic and proteolytic activities, it has been implicated as a prognostic marker in many tumor types. Cathepsin D is expressed in epithelial cells as well as in macrophages.

    • Synonyms

      Cathepsin D, EC 3.4.23.5, CTSD, CPSD, CLN10, MGC2311.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store vial at -20°C to -80°C. When stored at the recommended temperature, this protein is stable for 12 months.Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      LVRIPLHKFT SIRRTMSEVG GSVEDLIAKG PVSKYSQAVP AVTEGPIPEV LKNYMDAQYY GEIGIGTPPQ CFTVVFDTGS SNLWVPSIHC KLLDIACWIH HKYNSDKSST YVKNGTSFDI HYGSGSLSGY LSQDTVSVPC QSASSASALG GVKVERQVFG EATKQPGITF IAAKFDGILG MAYPRISVNN VLPVFDNLMQ QKLVDQNIFS FYLSRDPDAQ PGGELMLGGT DSKYYKGSLS YLNVTRKAYW QVHLDQVEVA SGLTLCKEGC EAIVDTGTSL MVGPVDEVRE LQKAIGAVPL IQGEYMIPCE KVSTLPAITL KLGGKGYKLS PEDYTLKVSQ AGKTLCLSGF MGMDIPPPSG PLWILGDVFI GRYYTVFDRD NNRVGFAEAA RLHHHHHH

    • Enzymatic Activity

      > 20 pmol/min/ug, defined as the amount of enzyme which cleaves 1pmol of Mca-PLGLDpa-AR-NH2/min at pH-3.5 at 25C.

    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.

    Ctsd Human
  • View Data Sheet

    Name :

    Calcitonin Salmon

    Description:

    Calcitonin Acetate Salmon

    CT, KC, CGRP, CALC1, CGRP1, CGRP-I, MGC126648, katacalcin, Calcitonin gene-related peptide 1 precursor, Calcitonin gene-related peptide I.

    Product # :

    HOR-262

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    Description

    Calcitonin Acetate (Salmon) is a synthetic polypeptide of 32 amino acids in the same linear sequence that is found in calcitonin of salmon origin. The Molecular Formula is C145H240N44O48S2. Calcitonin Molecular Weight: 3431.9 Dalton.

    Formulation

    The calcitonin 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

      Calcitonin (CT) is a peptide hormone produced by the parafollicular cells of the thyroid gland in mammals and by the ultimobranchial gland of birds and fish. Salmon calcitonin (sCT), which is more potent and longer lasting than human CT, has been used widely for the treatment of osteoporosis, paget's disease, hypercalcemic shock and chronic pain in terminal cancer patients. sCT is one of the many bioactive peptides that require C-terminal amidation for full biological activity.

    • Synonyms

      CT, KC, CGRP, CALC1, CGRP1, CGRP-I, MGC126648, katacalcin, Calcitonin gene-related peptide 1 precursor, Calcitonin gene-related peptide I.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Calcitonin Acetate (Salmon) has an amino acid sequence of: Cys-Ser-Asn-Leu-Ser-Thr-Cys-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Thr-Gly-Ser-Gly-Thr-Pro-NH2.

    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.

    Calcitonin Salmon
  • View Data Sheet

    Name :

    PHOSPHO1 Human

    Description:

    Phosphatase Orphan-1 Human Recombinant

    Phosphoethanolamine/phosphocholine phosphatase, Phosphatase, Orphan 1, EC 3.1.3.75, Phospho1.

    Product # :

    ENZ-363

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    Description

    Human Phospho1 Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 295 amino acids and having a molecular mass of 31.3 kDa. The Human Phospho1 is fused to a 14 aa His tag at N-Terminus. Human Phosphocholine Phosphatase is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 30mM acetate buffer pH-4.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PHOSPHO1 is involved in mineralization process & plays a role in bone and cartilage matrix mineralization.
      PHOSPHO1 is expressed at sites of mineralization in bone and cartilage. Highly expressed in osteoblast cell line SaOS-2 which produces a mineralized matrix.
      Orphan-1 is collagen type -2 is specific for cartilaginous tissues. Orphan1 is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces.
      Phosphoethanolamine (2-O3POCH2CH2NH3) is a key intermediate in the formation of cephalins, it is formed in liver and brain by phosphorylation of ethanolamine.
      PHOSPHO2 and PHOSPHO1 suggest subtle differences in the charge distributions around the putative substrate entry site and in the location of potential H-bond donors.
      PHOSPHO1 exhibits high specific phosphoethanolamine and phosphocholine phosphatase activities PHOSPHO1 is a phosphatase enzyme for which expression is upregulated in mineralizing cells. PHOSPHO1 has been implicated in the generation of Pi for matrix mineralization, a process central to skeletal development. PHOSPHO1 is a member of the haloacid dehalogenase (HAD) superfamily of Mg2+-dependent hydrolases. PHOSPHO1 exhibits high specific activities toward phosphoethanolamine (PEA) and phosphocholine (PCho).

    • Synonyms

      Phosphoethanolamine/phosphocholine phosphatase, Phosphatase, Orphan 1, EC 3.1.3.75, Phospho1.

    • Physical Appearance

      Filtered 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 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this protein is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMSGCFP VSGLRCLSRD GRMAAQGAPR FLLTFDFDET IVDENSDDSI VRAAPGQRLP ESLRATYREG FYNEYMQRVF KYLGEQGVRP RDLSAIYEAI PLSPGMSDLL QFVAKQGACF EVILISDANT FGVESSLRAA GHHSLFRRIL SNPSGPDARG LLALRPFHTH SCARCPANMC KHKVLSDYLR ERAHDGVHFE RLFYVGDGAN DFCPMGLLAG GDVAFPRRGY PMHRLIQEAQ KAEPSSFRAS VVPWETAADV RLHLQQVLKSC.

    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.

    Phospho1 Human
  • View Data Sheet

    Name :

    CTF1 Mouse

    Description:

    Cardiotrophin-1 Mouse Recombinant

    CTF1, CT1, CT-1, Cardiophin 1.

    Product # :

    CYT-151

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    Description

    CTF1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 202 amino acids and having a molecular mass of 21.3kDa.The CTF1 Mouse 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 98.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of TF-1 cells was < 1.0ng/ml, corresponding to a specific activity of > 1,000,000units/mg.

    More Info

    • Introduction

      Cardiotrophin 1 (CT-1) is a 201 amino acid member of the interleukin-6 superfamily. It was identified by its ability to induce hypertrophic response in cardiac myocytes. CT-1 mRNA levels were found both in cardiac myocytes and in cardiac nonmyocytes. CT 1 was also detected in abundance in normal adult human lung and was expressed in both fetal and adult airway smooth muscle cells. CT 1 activates gp130 dependent signaling and stimulates the Janus kinase/signal transducers and activators of transcription (JAK/STAT) pathway to transduce hypertrophic and cytoprotective signals in cardiac myocytes.
      CT 1 has also a neurotrophic function. CTF1 deficiency causes increased motoneuron cell death in spinal cord and brainstem nuclei of mice during a period between embryonic day 14 and the first postnatal week. Moreover, CT-1 is a hepatocyte survival factor that efficiently reduces hepatocellular damage in animal models of acute liver injury. Cardiotrophin 1 expression is augmented after hypoxic stimulation and it can protect cardiac cells when added either prior to simulated ischaemia or at the time of reoxygenation following simulated ischaemia. Cardiotrophin 1 can induce expression of the protective heat shock proteins (hsps) in cardiac cells.
      Cardiotrophin-1 increased ventricular expression of ANP, brain natriuretic peptide (BNP) and angiotensinogen mRNA.
      Cardiophin 1 levels were significantly elevated in patients with heart failure, patients with dilatative cardiomyopathy, moderate/severe mitral regurgitation, stable and unstable angina and after acute myocardial infarction.

    • Synonyms

      CTF1, CT1, CT-1, Cardiophin 1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CTF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CTF1 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 CTF1 in sterile 4mM HCl to a concentration of 0.1-0.5 mg/ml. Stock solutions should be apportioned into working aliquots and stored at <-200C. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      SQREGSLEDH QTDSSISFLP HLEAKIRQTH NLARLLTKYA EQLLEEYVQQ QGEPFGLPGF SPPRLPLAGL SGPAPSHAGL PVSERLRQDA AALSVLPALL DAVRRRQAEL NPRAPRLLRS LEDAARQVRA LGAAVETVLA ALGAAARGPG PEPVTVATLF TANSTAGIFS AKVLGFHVCG LYGEWVSRTE GDLGQLVPGG VA

    • Background

      What is the molecular weight/Mw of CTF1 Protein?
      CTF1 Protein has a total Mw of 21.3kDa.

      What is the source or expression system of CTF1 Protein?
      Escherichia Coli.

      What is the Purity of CTF1 Protein?
      CTF1 Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of CTF1 Protein?
      The ED50 as determined by the dose-dependent proliferation of TF-1 cells was < 1.0ng/ml, corresponding to a specific activity of > 1,000,000units/mg.

      What is the amino acid sequence of CTF1 Protein?
      SQREGSLEDH QTDSSISFLP HLEAKIRQTH NLARLLTKYA EQLLEEYVQQ QGEPFGLPGF SPPRLPLAGL SGPAPSHAGL PVSERLRQDA AALSVLPALL DAVRRRQAEL NPRAPRLLRS LEDAARQVRA LGAAVETVLA ALGAAARGPG PEPVTVATLF TANSTAGIFS AKVLGFHVCG LYGEWVSRTE GDLGQLVPGG VA

      What applications can CTF1 Protein be used in?
      CTF1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CTF1 Protein?
      The endotoxin level is minimal, CTF1 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.

    Ct 1 Mouse
  • View Data Sheet

    Name :

    CXCL17 Human, His

    Description:

    VEGF Co-regulated Chemokine 1, His Tag Human Recombinant

    Dcip1, DMC, MGC138300, UNQ473, VCC-1, VCC1, VEGF coregulated chemokine 1, C-X-C motif chemokine 17, Dendritic cell and monocyte chemokine-like protein.

    Product # :

    CHM-024

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    • SDS-PAGE

    Description

    CXCL17 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 119 amino acids (22-119 a.a) and having a molecular mass of 13.7kDa.CXCL17 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CXCL17 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    SDS-PAGE

    CXCL17 Human, His-SDS-PAGE - Product image 1

    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

      Dcip1, DMC, MGC138300, UNQ473, VCC-1, VCC1, VEGF coregulated chemokine 1, C-X-C motif chemokine 17, Dendritic cell and monocyte chemokine-like protein.

    • 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 MSSLNPGVAR GHRDRGQASR RWLQEGGQEC ECKDWFLRAP RRKFMTVSGL PKKQCPCDHF KGNVKKTRHQ RHHRKPNKHS RACQQFLKQC QLRSFALPL.

    • Background

      What is the molecular weight/Mw of CXCL17 HUMAN, HIS Protein?
      CXCL17 HUMAN, HIS Protein has a total Mw of 13.7kDa.

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

      What is the Purity of CXCL17 HUMAN, HIS Protein?
      CXCL17 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL17 HUMAN, HIS Protein?
      The biological functionality of CXCL17 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CXCL17 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MSSLNPGVAR GHRDRGQASR RWLQEGGQEC ECKDWFLRAP RRKFMTVSGL PKKQCPCDHF KGNVKKTRHQ RHHRKPNKHS RACQQFLKQC QLRSFALPL.

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

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

    Cxcl17 Human His
  • View Data Sheet

    Name :

    PTX2 Mouse

    Description:

    Pentraxin-2 Mouse Recombinant

    Serum amyloid P-component, SAP, Apcs, Sap, Ptx2.

    Product # :

    PRO-2598

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    Description

    PTX2 Mouse Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 210 amino acids (21-224 a.a) and having a molecular mass of 24.6kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). PTX2 is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293.

    Formulation

    PTX2 protein solution (0.25mg/ml) contains 10% glycerol in Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PTX-2 or Pentraxin-2 is a phylogenetically conserved protein, commonly moving with homopentameric blood protein or with a protein that recognizes receptors of the innate immune system. The protein’s specific binding abilities may show that PTX-2 is specially bound in sites where injury accrued, therefore helps to eliminate damaged tissue by ways that are not phlogistics.

    • Synonyms

      Serum amyloid P-component, SAP, Apcs, Sap, Ptx2.

    • 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

      QTDLKRKVFV FPRESETDHV KLIPHLEKPL QNFTLCFRTY SDLSRSQSLF SYSVKGRDNE LLIYKEKVGE YSLYIGQSKV TVRGMEEYLS PVHLCTTWES SSGIVEFWVN GKPWVKKSLQ REYTVKAPPS IVLGQEQDNY GGGFQRSQSF VGEFSDLYMW DYVLTPQDIL FVYRDSPVNP NILNWQALNY EINGYVVIRP RVWDHHHHHH.

    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.

    Ptx2 Mouse
  • View Data Sheet

    Name :

    TPO Mouse, HEK

    Description:

    Thrombopoietin Mouse Recombinant, HEK

    Thpo, C-mpl ligand,ML, Megakaryocyte colony-stimulating factor, Megakaryocyte growth and development factor, MGDF, Myeloproliferative leukemia virus oncogene ligand, Mgdf, Ml, Mpllg, Tpo, thrombopoietin isoform 1.

    Product # :

    CYT-1157

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    Description

    TPO Mouse Recombinant produced in HEK293 cells is a single, non-glycosylated polypeptide chain containing 341 amino acids ( 22-356 a.a) and having a molecular mass of 36.4kDa. TPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    HEK293.

    Formulation

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

    Purity

    Measured in a cell proliferation assay using MO7e human megakaryocytic leukemic cells. The ED50 range ≤4ng/ml.

    Biological Activity

    Measured by its ability to agglutinate human red blood cells. The ED50 for this effect is ≥ 25ug/ml. 

    More Info

    • Introduction

      Thrombopoietin or TPO or MGDF, is a protein (glycoprotein hormone) that can be found in the liver and kidney tissues. TPO regulates the creation of platelets. The protein enhances the production & differentiation of cells such as megakaryocytes that are part of the bone marrow cells that secretes a wide number of platelets. The cellular development process that ends up in the production of platelet calls (Megakaryocytopoiesis). Humoral growth factor is needed for the megakaryocyte proliferation & maturation of megakaryocyte, not apart from thrombopoiesis.

    • Synonyms

      Thpo, C-mpl ligand,ML, Megakaryocyte colony-stimulating factor, Megakaryocyte growth and development factor, MGDF, Myeloproliferative leukemia virus oncogene ligand, Mgdf, Ml, Mpllg, Tpo, thrombopoietin isoform 1.

    • 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

      SPVAPACDPR LLNKLLRDSH LLHSRLSQCP DVDPLSIPVL LPAVDFSLGE WKTQTEQSKA QDILGAVSLL LEGVMAARGQ LEPSCLSSLL GQLSGQVRLL LGALQGLLGT QLPLQGRTTA HKDPNALFLS LQQLLRGKVR FLLLVEGPTL CVRRTLPTTA VPSSTSQLLT LNKFPNRTSG LLETNFSVTA RTAGPGLLSR LQGFRVKITP GQLNQTSRSP VQISGYLNRT HGPVNGTHGL FAGTSLQTLE ASDISPGAFN KGSLAFNLQG GLPPSPSLAP DGHTPFPPSP ALPTTHGSPP QLHPLFPDPS TTMPNSTAPH PVTMYPHPRN LSQETHHHHH 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.

    Thrombopoietin Mouse
  • View Data Sheet

    Name :

    S100b Mouse, His

    Description:

    S100 Calcium Binding Protein B Mouse Recombinant, His Tag

    Protein S100-B, S-100 protein beta chain, S-100 protein subunit beta, S100 calcium-binding protein B, Bpb, AI850290, MGC74317, S100b.

    Product # :

    PRO-853

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    Description

    S100B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 92 amino acids (1-112 a.a.) and having a molecular mass of 12.8 kDa. The Mouse S100B is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    S100B Mouse solution containing 20mM Tris-HCl pH-8, 1mM DTT & 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      S100B faintly binds calcium but binds zinc extremely strongly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. S100B binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction participates in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling.

    • Synonyms

      Protein S100-B, S-100 protein beta chain, S-100 protein subunit beta, S100 calcium-binding protein B, Bpb, AI850290, MGC74317, S100b.

    • 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 MSELEKAMVA LIDVFHQYSG REGDKHKLKK SELKELINNE LSHFLEEIKE QEVVDKVMET LDEDGDGECD FQEFMAFVAM VTTACHEFFE HE.

    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.

    S100B Mouse
  • View Data Sheet

    Name :

    CXCL7 Rat

    Description:

    Neutrophil Activating Protein-2 Rat Recombinant (CXCL7)

    Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    Product # :

    CHM-269

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    • More Info

    Description

    NAP-2 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 62 amino acids and having a molecular mass of 6.8kDa.The NAP 2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NAP-2 protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4.

    Purity

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

    Biological Activity

    Measured by its ability to chemoattract BaF3 mouse pro-B cells transfected with human CXCR2. The ED50 for this effect is less than 10ng/ml, corresponding to a specific activity of 100,000units/mg.

    More Info

    • Introduction

      Chemokine (C-X-C motif) ligand (CXCL7) is a small cytokine belonging to the CXC chemokine family. It is a protein that is released in large amounts from platelets following their activation. It stimulates various processes including mitogenesis, synthesis of extracellular matrix, glucose metabolism and synthesis of plasminogen activator.

    • Synonyms

      Platelet basic protein, PBP, Small inducible cytokine B7, CXCL7, Leukocyte-derived growth factor, LDGF, Macrophage-derived growth factor, MDGF, pro-platelet basic protein (chemokine (C-X-C motif) ligand 7), TC1, TC2, TGB, TGB1, B-TG1, CTAP3, NAP-2, SCYB7, THBGB, LA-PF4, THBGB1, Beta-TG, CTAPIII, CTAP-III.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NAP-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL7 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 NAP-2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      IELRCRCTNT LSGIPLNSIS RVNVFRPGAH CDNVEVIATL KNGKEVCLDP TAPMIKKIVK KI.

    • Background

      What is the molecular weight/Mw of CXCL7 RAT Protein?
      CXCL7 RAT Protein has a total Mw of 6.8kDa.

      What is the source or expression system of CXCL7 RAT Protein?
      Escherichia Coli.

      What is the Purity of CXCL7 RAT Protein?
      CXCL7 RAT Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CXCL7 RAT Protein?
      Measured by its ability to chemoattract BaF3 mouse pro-B cells transfected with human CXCR2. The ED50 for this effect is less than 10ng/ml, corresponding to a specific activity of 100,000units/mg.

      What is the amino acid sequence of CXCL7 RAT Protein?
      IELRCRCTNT LSGIPLNSIS RVNVFRPGAH CDNVEVIATL KNGKEVCLDP TAPMIKKIVK KI.

      What applications can CXCL7 RAT Protein be used in?
      CXCL7 RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CXCL7 RAT Protein?
      The endotoxin level is minimal, CXCL7 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.

    Nap 2 Rat
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