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Search results

1000 results found for “Serglycin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    TROVE2 Bovine

    Description:

    TROVE Domain Family, Member 2, Bovine

    60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

    Product # :

    PRO-111

    Price :

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    Description

    TROVE2 is a natural protein having a molecular mass of 60kDa. TROVE2 is purified from bovine tissues by protein-chemical methods.

    Source

    Bovine tissues.

    Formulation

    TROVE2 is supplied in 20mM Tris/HCl buffer pH-7.5, 150mM NaCl, 2mM MgCl2, 0.2mM DTT, 0.1mM PMSF and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Ro 60 kDa autoantigen is an RNA-binding protein that binds to several small cytoplasmic RNA molecules known as Y RNAs. SSA2 may stabilize these RNAs from degradation. Sera taken from patients with Systemic Lupus Erythematosus (SLE) often contains antibodies that react with the normal cellular SSA2 protein as if this antigen was foreign.

    • Synonyms

      60 kDa SS-A/Ro ribonucleoprotein, 60 kDa ribonucleoprotein Ro, RoRNP, 60 kDa Ro protein, Ro 60 kDa autoantigen, TROVE domain family member 2, Sjoegren syndrome type A antigen, SS-A, Sjoegren syndrome antigen A2, TROVE2, RO60, SSA2, RO-60.

    • 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 IgG-type human auto-antibodies. 2. Standard ELISA test (checkerboard analysis of positive/negative sera panels); immunodot test with positive/negative sera panels.

    • coating concentration

      0.2-0.6 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for biotinylation and iodination.

    • Applications

      Western blot with SLE sera (secondary Sjogren’s syndrome).

    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.

    Trove2 Bovine
  • View Data Sheet

    Name :

    Batroxobin

    Description:

    Batroxobin

    Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Batroxobin.

    Product # :

    PRO-2146

    Price :

    Quantity :

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    Description

    Batroxobin, isolated from Bothrops atrox snake venom, has an Mw of approximately 43kDa.

    Formulation

    The Batroxobin protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

    More Info

    • Introduction

      Batroxobin is a serin protease that reduces fibronogen levels and is originally extracted from snake venom of Bothrops Atrox. Batroxobin is used in defibrinogenation and thrombolysis and also has an effect on c-fos gene and growth factor.
      Batroxobin can efficiently restrain proliferation of VSMCs, by blocking the release and uptake of Ca2+, thus influencing [Ca2+]i.
      Batroxobin converts fibrinogen to fibrin through the restricted release of fibrinopeptide-A from fibrinogen to promote blood to clot. Unlike thrombin, it is not affected by heparin and hirudin.

    • Synonyms

      Thrombin-like enzyme batroxobin, EC 3.4.21.74, BX, Bothrops atrox serine proteinase, Venombin-A, Batroxobin.

    • Physical Appearance

      Sterile Filtered white lyophilized powder.

    • Stability

      Store the lyophilized Batroxobin between 2-8°C. Do not freeze!

    • Solubility

      It is recommended to reconstitute the lyophilized Batroxobin in sterile 18MΩ-cm H2O not less than 100µg/ml or more than 10mg/ml solutions.

    • Unit Definition

      100BU [Batroxobin Units]=1mg.

    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.

    Batroxobin Native
  • View Data Sheet

    Name :

    TAC3 Human

    Description:

    Tachykinin-3 Human Recombinant

    Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.

    Product # :

    PRO-716

    Price :

    Quantity :

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    Description

    TAC3 Human Recombinant fused with 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (17-121 a.a.) and having a molecular mass of 13.8kDa.The TAC3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The TAC3 solution contains 20mM Tris-HCl buffer (pH 8.0) and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tachykinin-3 belongs to the substance P-related tachykinin family. Tachykinins are active peptides that stimulate neurons, induce behavioral responses, are effective vasodilators and secretagogues, and contract (directly or indirectly) many smooth muscles. TAC3 and its receptor are essential switches of regulator of human puberty, regulated by the brain through the release of the GnRH which starts a chain of processes which eventually lead to the production of sex hormones.
      During pregnancy, the expression of TAC3 is restricted to the outer syncytiotrophoblast of the placenta, significant concentrations of TAC3 can be identified in plasma as early as week 9, and plasma concentrations of TAC3 are grossly elevated in pregnancy-induced hypertension and pre-eclampsia. Higher Tachykinin-3 concentrations in normotensive pregnant women may be caused by the advanced gestational age and/or the result of a negative interaction of other vasoactive substances. TAC3 has a role in the continuance of high placental blood flow in normal pregnancy.

    • Synonyms

      Tachykinin-3, ZNEUROK1, Neurokinin-B, NKB, Neuromedin-K, TAC3, NKNB, PRO1155.

    • 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 QSFGAVCKEP QEEVVPGGGR SKRDPDLYQL LQRLFKSHSS LEGLLKALSQ ASTDPKESTS PEKRDMHDFF VGLMGKRSVQ PDSPTDVNQE NVPSFGILKY PPRAE.

    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.

    Tac3 Human
  • View Data Sheet

    Name :

    TOR1A Human

    Description:

    Torsin Family 1 Member A Human Recombinant

    DQ2, DYT1, Torsin-1A, Dystonia 1 protein, Torsin family 1 member A, TOR1A.

    Product # :

    PRO-1430

    Price :

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    Description

    TOR1A Human Recombinant produced in E. coli is a single polypeptide chain containing 333 amino acids (21-332) and having a molecular mass of 38kDa. TOR1A is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TOR1A solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      TOR1A which is a member of the AAA family of adenosine triphosphatases (ATPases) is associated to the Clp protease/heat shock family and is expressed highly in the substantia nigra pars compacta.TOR1A functions as a molecular chaperone assisting in the suitable folding of secreted and/or membrane proteins. Mutations in TOR1A result in the autosomal dominant disorder, torsion dystonia one.

    • Synonyms

      DQ2, DYT1, Torsin-1A, Dystonia 1 protein, Torsin family 1 member A, TOR1A.

    • 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 MVEPISLGLA LAGVLTGYIY PRLYCLFAEC CGQKRSLSRE ALQKDLDDNL FGQHLAKKII LNAVFGFINN PKPKKPLTLS LHGWTGTGKN FVSKIIAENI YEGGLNSDYV HLFVATLHFP HASNITLYKD QLQLWIRGNV SACARSIFIF DEMDKMHAGL IDAIKPFLDY YDLVDGVSYQ KAMFIFLSNA GAERITDVAL DFWRSGKQRE DIKLKDIEHA LSVSVFNNKN SGFWHSSLIH RNLIDYFVPF LPLEYKHLKM CIRVEMQSRG YEIDEDIVSR VAEEMTFFPK EERVFSDKGC KTVFTKLDYY YDD.

    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.

    Tor1A Human
  • View Data Sheet

    Name :

    BMP 4 Human

    Description:

    Bone Morphogenetic Protein-4 Human Recombinant

    BMP4, ZYME, BMP2B, BMP2B1.

    Product # :

    CYT-361

    Price :

    Quantity :

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    • description
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    • formulation
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    Description

    Bone Morphogenetic Protein-4 Human Recombinant produced in E.Coli is a monomeric, non-glycosylated, Polypeptide chain containing 116 amino acids and having a molecular mass of 13kDa. The BMP-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-4 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM Na2CO3 buffer, pH 9.0.

    Purity

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

    More Info

    • Introduction

      The protein encoded by this gene is a member of the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. The superfamily includes large families of growth and differentiation factors. Bone morphogenetic proteins were originally identified by an ability of demineralized bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site. This particular family member plays an important role in the onset of endochondral bone formation in humans, and a reduction in expression has been associated with a variety of bone diseases, including the heritable disorder Fibrodysplasia Ossificans Progressiva. Alternative splicing in the 5' untranslated region of this gene has been described and three variants are described, all encoding an identical protein.

    • Synonyms

      BMP4, ZYME, BMP2B, BMP2B1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Bone Morphogenetic Protein-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP4 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 Bone Morphogenetic Protein-4 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

    • Background

      What You Should Know About Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant

      As part of the transforming growth factor-beta (TGF-β) superfamily, Bone morphogenetic protein-4 (BMP-4) participates in multiple developmental processes, from embryogenesis to bone and cartilage formation.

      Since this signaling protein is involved in many physiological processes, its laboratory-produced version has been studied for different medical applications. Additionally, a reduction in BMP-4 expression has been associated with multiple diseases, leading to further research into its potential therapeutic benefits.

      Are you interested in learning more about Bone Morphogenetic Protein-4 (BMP-4) human recombinant? Read on to find more information!

      How Does Bone Morphogenetic Protein-4 (BMP-4) Work?

      Bone Morphogenetic Protein-4 (BMP-4) regulates microRNAs miR-494 and miR-126-5p expression, controlling endothelial cells' involvement and function in angiogenesis. As such, it has diverse effects on cell growth, differentiation, and survival.

      The Role of BMP-4

      This protein emits signals that promote the formation of different tissues and organs, including the bones and cartilage, kidneys, teeth, and the neural tube. In other words, it's essential for the development of the heart, skeleton, and central nervous system.

      However, the role of BMP-4 goes beyond these processes. It participates in different physiological activities, such as:

      • Embryonic development
      • Wound healing
      • Bone remodeling
      • Immune response modulation
      • Tissue repair
      • Cardiac development and function

      What Is Bone Morphogenetic Protein-4 (BMP-4) Human Recombinant?

      To replicate the effects of the BMP4 found in humans and explore its possible therapeutic applications, many laboratories have started producing this protein in Chinese hamster ovary (CHO) cells.

      As mentioned, decreased BMP-4 expression has been associated with different diseases, including bone disorders, fibrosis, and cancer, which can cause other conditions, such as organ dysfunction.

      More research is needed, but BMP-4 human recombinant (rhBMP4) produced in CHO has the potential to address these diseases and could be used for other medical applications. These are some examples:

      • Cancer therapy
      • Development of engineered tissues and organs
      • Bone regeneration for the treatment of osteoporosis and nonunion fractures
      • Bone growth and fusion in spinal fusion surgeries (the U.S. Food and Drug Administration approved some bone morphogenetic proteins for these procedures)
      • Promotion of tissue repair and regeneration

      Final Thoughts BMP-4

      Although BMP-4 human recombinant produced in CHO offers potential benefits, several challenges remain, including possible side effects, as high doses can cause inflammation, bone overgrowth, and other issues.

      However, the long-term effects of rhBMP4 are still under investigation. Further research will provide solutions to address these challenges and allow experts to explore this laboratory-produced protein's power in different medical fields.

      What is the molecular weight/Mw of BMP4 Protein?
      BMP4 Protein has a total Mw of 13kDa.

      What is the source or expression system of BMP4 Protein?
      Escherichia Coli.

      What is the Purity of BMP4 Protein?
      BMP4 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP4 Protein?
      The biological functionality of BMP4 Protein will be determined in the future.

      What is the amino acid sequence of BMP4 Protein?
      SPKHHSQRAR KKNKNCRRHS LYVDFSDVGW NDWIVAPPGY QAFYCHGDCP FPLADHLNST NHAIVQTLVN SVNSSIPKAC CVPTELSAIS MLYLDEYDKV VLKNYQEMVV EGCGCR.

      What applications can BMP4 Protein be used in?
      BMP4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP4 Protein?
      The endotoxin level is minimal, BMP4 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.

    Bmp4 Human
  • View Data Sheet

    Name :

    Fertirelin

    Description:

    Fertirelin

    Product # :

    HOR-037

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    Description

    Fertirelin Synthetic is a single, non-glycosylated polypeptide chain containing 9 amino acids, having a molecular mass of 1153.31 Dalton and a Molecular formula of C55H76N16O12.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 97.0% as determined by analysis by RP-HPLC.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Pyr-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-NHEt.

    • Background

      Fertirelin, a potent gonadotropin-releasing hormone (GnRH) analogue, is crucial for fertility regulation in animals. This research paper endeavors to expound on the biochemical attributes of fertirelin and its potential therapeutic applications in veterinary medicine.

      Fertirelin, a synthetic analogue of the natural gonadotropin-releasing hormone, plays a fundamental role in fertility regulation in veterinary medicine. It stimulates the secretion of luteinizing hormone and follicle-stimulating hormone, crucial for reproduction (Kotwica et al., 2005). This paper aims to delve into the biochemical characteristics of fertirelin and its potential applications.

      Fertirelin, as a GnRH analogue, elicits its action by binding to GnRH receptors located on pituitary gonadotroph cells. This leads to the release of luteinizing hormone and follicle-stimulating hormone, key players in ovulation and spermatogenesis (Kotwica et al., 2005).

      In the realm of veterinary medicine, fertirelin is primarily used for treating ovarian follicular cysts in dairy cattle (Bosu & Peter, 1987). Its potent stimulatory effect on gonadotropin secretion facilitates ovulation and contributes to fertility management strategies.

      The potential of fertirelin extends beyond the current applications. Further research into the precise mechanism of action and potential side effects can enhance its utilization. Overall, fertirelin presents a powerful tool in veterinary reproductive medicine, making it a focal point of interest for future studies.

    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.

    Fertirelin
  • View Data Sheet

    Name :

    Shiga Like Toxin 1

    Description:

    Shiga Like Toxin-1 Subunit B Recombinant

    Product # :

    STX-001

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    Description

    Recombinant Shiga Like Toxin-1 Subunit B is produced from E.Coli O157:H7 amino acids 2-90 of the Shiga Like Toxin-1 Subunit B.The Shiga Like Toxin 1 protein is fused to a 6xHis tag at its N-terminus and purified by proprietary chromatographic technique.

    Source

    Escherichia Coli.

    Formulation

    Phosphate buffered saline and 25mM K₂CO₃.

    Purity

    Protein is >95% pure as determined by 12% PAGE (coomassie staining).

    More Info

    • Introduction

      Shiga-like toxin (verotoxin) is a toxin produced by some strains of Escherichia coli. Shiga-like toxin is named for its similarity to the AB5-type Shiga toxin produced by the bacteria Shigella dysenteriae. There are two known types-SLT1 and SLT2. The Shiga-like toxin is linked with hemolytic-uremic syndrome. Shiga-like toxin requires highly specific receptors on the cells' surface in order to attach and enter the cell. Species such as cattle, swine, and deer which do not carry these receptors may harbor toxigenic bacteria without any ill effect, dropping them in their feces, from where they may be distributed to humans. Shiga Like Toxin-1 Subunit B has nontoxic action, it is the functional region which binds to the receptor. The Shiga Like Toxin-1 Subunit B can be useful in vaccine study, antibody test and other functional research.

    • 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.

    • Purification Method

      Purified by affinity chromatographic technique.

    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.

    Shiga Like Toxin 1
  • View Data Sheet

    Name :

    CX3CL1 Human, Sf9

    Description:

    Fractalkine (CX3CL1) Human Recombinant, Sf9

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

    Product # :

    CHM-042

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    • SDS-PAGE

    Description

    Fractalkine Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 323 amino acids (25-339aa) and having a molecular mass of 34.3kDa.Fractalkine is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Fractalkine solution (1 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    CX3CL1 Human, Sf9-SDS-PAGE - Product image 1

    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. 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 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

      QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
      AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
      QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
      PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
      MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH

    • Background

      What is the molecular weight/Mw of CX3CL1 HUMAN, SF9 Protein?
      CX3CL1 HUMAN, SF9 Protein has a total Mw of 34.3kDa.

      What is the source or expression system of CX3CL1 HUMAN, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of CX3CL1 HUMAN, SF9 Protein?
      CX3CL1 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CX3CL1 HUMAN, SF9 Protein?
      The biological functionality of CX3CL1 HUMAN, SF9 Protein will be determined in the future.

      What is the amino acid sequence of CX3CL1 HUMAN, SF9 Protein?
      QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
      AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
      QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
      PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
      MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH

      What applications can CX3CL1 HUMAN, SF9 Protein be used in?
      CX3CL1 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CX3CL1 HUMAN, SF9 Protein?
      The endotoxin level is minimal, CX3CL1 HUMAN, SF9 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.

    Cx3Cl1 Human
  • View Data Sheet

    Name :

    Leptin qA Human, PEG

    Description:

    Leptin Quadruple Antagonist Pegylated Human Recombinant

    Product # :

    CYT-1251

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    Description

    Leptin Pegylated Quadruple Antagonist Human Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and an additional Ala at N-terminus acids. The Human Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Human Leptin Pegylated Quadruple Antagonist was mutated, resulting in D23L/L39A/D40A/F41A that was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Human Leptin Pegylated Quadruple Antagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Human Leptin Pegylated Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is 6-8 fold lower than the non-pegylated human leptin antagonist but in vivo it has profound weight gain effect (as compared to the non-pegylated human leptin antagonist), resulting mainly from increased food intake. The in vivo activity of human pegylated super leptin antagonist was compared to that of human pegylated leptin antagonist is 9-27 fold higher.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Human Leptin Pegylated Quadruple Antagonist although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 and up to 2mM of Human pegylated leptin antagonist and filter sterilization Human pegylated leptin antagonist can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Human Leptin Pegylated Quadruple Antagonist in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Background

      Leptin is a~16 kDa protein which is encoded by the obese gene. Leptin is a hormone which participates in regulating body weight, reproductive function and metabolism. leptin is expressed predominantly by adipocytes, which supports the idea that body weight is sensed as the total mass of fat in the body. Smaller amounts of leptin are also secreted by cellsin the epithelium of the stomach and in the placenta. Leptin receptors are highly expressed in areas of the hypothalamus which regulates body weight, as well as in T lymphocytes and vascular endothelial cells.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.88 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Human Qa Peg
  • View Data Sheet

    Name :

    Leptin qA Ovine, PEG

    Description:

    Leptin Quadruple Antagonist Pegylated Ovine Recombinant

    Product # :

    CYT-1246

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    Description

    Leptin Antagonist Quadruple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino acids and additional Ala at N-terminus. The Ovine Leptin antagonist was mutated, resulting in D23L/L39A/D40A/F41A mutant. The Ovine Leptin antagonist is bound to 20 kDa mono-PEG at N-terminus, resulting in 35.6 kDa. The Ovine Leptin Quadruple anatagonist Pegylated runs as a 48 kDa due to enlarged hydrodymanic volume. Leptin Antagonist Quadruple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The Ovine Leptin Quadruple anatagonist was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 95.0% as determined by:

    (a) Gel filtration analysis.

    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated Ovine Leptin Quadruple Antagonist inhibits leptin-induced proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Pegylated recombinant Ovine leptin antagonist in vitro activity is 6-8 fold lower than the non-pegylated recombinant super Ovine leptin antagonist but is 15 fold higher as compared to pegylated recombinant super active ovine leptin antagonist.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 mg/ml and up to 2mM and filter sterilization LEP mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin Antagonist Quadruple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted with other aqueous solutions.

    • Background

      Leptin is mainly produced by adipocytes. Leptin’s main part is to regulate long-term energy balance. Leptin is encoded by the LEP gene. Leptin effects mostly on leptin receptors in the cell mambrane of various cells in the human body. The leptin receptor can be found on a various cell types. The leptin receptor is a single-transmembrane-domain type 1 cytokine receptor. leptin levels influence satiety, appetite and triggers behaviours which save energy. High leptin levels are interpreted by the brain that energy reserves are high, whereas low leptin levels means that energy reserves are low, in the process adapting the organism to starvation through a variety of metabolic, neurobiochemical, endocrine and behavioral change.

    • Protein content

      Protein quantization was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.2 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Antagonist Peg Ovine
  • View Data Sheet

    Name :

    Borrelia Spielmanii OspC

    Description:

    Borrelia Spielmanii Outer Surface Protein C Recombinant

    Product # :

    BOR-009

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    Description

    Recombinant Borrelia Spielmanii Outer Surface Protein C produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 24kDa. Borrelia Spielmanii OspC is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Borrelia Spielmanii OspC is supplied in 20mM HEPES buffer pH-8, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Borrelia belongs to a genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mainly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The main Borrelia species causing Lyme disease are Borrelia burgdorferi, Borrelia afzelii, and Borrelia garinii. The Borrelia genus members have a linear chromosome which is about 900 kbp in length as well as an excess of both linear and circular plasmids in the 5-220 kbp size range. The plasmids are atypical, as compared to most bacterial plasmids, since they contain many paralogous sequences, a large number of pseudogenes and, in some cases, essential genes. Moreover, a number of the plasmids have features suggesting that they are prophages.

    • 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 IgG- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma; suitable for LTT (lymphocyte transformation test).

    • Applications

      Western blot with patient sample.

    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.

    Borrelia Spielmanii Ospc
  • View Data Sheet

    Name :

    BSG Human

    Description:

    Basigin Human Recombinant

    Basigin isoform 2, 5F7, CD147, EMMPRIN, OK, TCSF, Leukocyte activation antigen M6, OK blood group antigen.

    Product # :

    PRO-2516

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    Description

    BSG produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 428 amino acids (22-207a.a.) and having a molecular mass of 47.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BSG is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    BSG protein solution (0.5mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Basigin Isoform 2 or BSG is a part of the immunoglobulin superfamily, it is a type 1 transmembrane protein which has a variety of Nand O- glycosylation. BSG has several ligands, such as integrins, cyclophilin proteins Cyp-A & CyP-B. The protein has a crucial role in intercellular recognition, it takes part in many immunologic processes, differentiation and cell development. Also, it regulates numerus cell processes such as production and release of expression of the mono-carboxylate transporter, spermatogenesis, etc. Basigin Isoform 2 promotes invasion, metastasis, growth and survival of malignant cells by producing and releasing matrix metalloproteinases nearby mesenchymal cells and tumor cells.

    • Synonyms

      Basigin isoform 2, 5F7, CD147, EMMPRIN, OK, TCSF, Leukocyte activation antigen M6, OK blood group antigen.

    • 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

      ADPAAGTVFT TVEDLGSKIL LTCSLNDSAT EVTGHRWLKG GVVLKEDALP GQKTEFKVDS DDQWGEYSCV FLPEPMGTAN IQLHGPPRVK AVKSSEHINE GETAMLVCKS ESVPPVTDWA WYKITDSEDK ALMNGSESRF FVSSSQGRSE LHIENLNMEA DPGQYRCNGT SSKGSDQAII
      TLRVRSHLAL 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.

    Basigin Human
  • View Data Sheet

    Name :

    Clusterin Human

    Description:

    Clusterin Human Recombinant

    CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    Product # :

    CYT-278

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    Description

    Clusterin Human Recombinant produced in HEK is a glycosylated, polypeptide chain containing 438 amino acids and having a molecular mass of 51.27 kDa. Clusterin (1-427 a.a.) is fused to 11 a.a. flag tag at c-terminal and purified by proprietary chromatographic techniques.

    Source

    293 cell line (Human embryonic kidney).

    Formulation

    Filtered (0.4 micron) and lyophilized PBS, pH 7.5.

    Purity

    Greater than 95% as determined by SDS PAGE.

    More Info

    • Introduction

      Clusterin also named Apolipoprotein J (APO-J) is a 75-80 kD disulfide-linked heterodimeric protein containing about 30% of N-linked carbohydrate rich in sialic acid but truncated forms targeted to the nucleus have also been identified.
      The precursor polypeptide chain is cleaved proteolytically to remove the 22-mer secretory signal peptide and subsequently between residues 227/228 to generate the a and b chains. These are assembled in anti-parallel to give a heterodimeric molecule in which the cysteine-rich centers are linked by five disulfide bridges and are flanked by two predicted coiled-coil a-helices and three predicted amphipathic a-helices.
      Across a broad range of species clusterin shows a high degree of sequence homology ranging from 70% to 80%. It is nearly ubiquitously expressed in most mammalian tissues and can be found in plasma, milk, urine, cerebrospinal fluid and semen.
      It is able to bind and form complexes with numerous partners such as immunoglobulins, lipids, bacteria, complement components, paraoxonase, beta amyloid, leptin and others. Clusterin has been ascribed a plethora of functions such as phagocyte recruitment, aggregation induction, complement attack prevention, apoptosis inhibition, membrane remodeling, lipid transport, hormone transport and/or scavenging, matrix metalloproteinase inhibition.
      A genuine function of clusterin has not been defined. One tempting hypothesis says that clusterin is an extracellular chaperone protecting cells from stress induced insults caused by degraded and misfolded protein precipitates.
      Clusterin is up- or down regulated on the mRNA or protein level in many pathological and clinically relevant situations including cancer, organ regeneration, infection, Alzheimer disease, retinitis pigmentosa, myocardial infarction, renal tubular damage, autoimmunity and others.

    • Synonyms

      CLI, AAG4, KUB1, SGP2, SGP-2, SP-40, TRPM2, MGC24903, Clusterin, Apolipoprotein J, Apo-J.

    • Physical Appearance

      Filtered, White, Lyophilized 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

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

    • Amino Acid Sequence

      DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEAAA DYKDDDDK.

    • Background

      What is the molecular weight/Mw of CLUSTERIN Protein?
      CLUSTERIN Protein has a total Mw of 51.27kDa.

      What is the source or expression system of CLUSTERIN Protein?
      293 cell line
      What is the Purity of CLUSTERIN Protein?
      CLUSTERIN Protein is >95% pure as determined by SDS-PAGE.

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

      What is the amino acid sequence of CLUSTERIN Protein?
      DQTVSDNELQ EMSNQGSKYV NKEIQNAVNG VKQIKTLIEK TNEERKTLLS NLEEAKKKKE DALNETRESE TKLKELPGVC NETMMALWEE CKPCLKQTCM KFYARVCRSGS GLVGRQLEE FLNQSSPFYF WMNGDRIDSL LENDRQQTHM LDVMQDHFSRA SSIIDELFQ DRFFTREPQD TYHYLPFSLP HRRPHFFFPK SRIVRSLMPF SPYEPLNFHA MFQPFLEMIH EAQQAMDIHF HSPAFQHPPT EFIREGDDDR TVCREIRHNS TGCLRMKDQC DKCREILSVD CSTNNPSQAKLRRELDESLQ VAERLTRKYN ELLKSYQWKM LNTSSLLEQL NEQFNWVSRL ANLTQGEDQYYLRVTTVASH TSDSDVPSGV TEVVVKLFDS DPITVTVPVE VSRKNPKFME TVAEKALQEY RKKHREEAAA DYKDDDDK.

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

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

    Clusterin Human Recombinant
  • View Data Sheet

    Name :

    Leuprorelin Human

    Description:

    Leuprolide Human

    Leuprolide, Leuprorelin.

    Product # :

    HOR-260

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    Description

    Leuprolide Human Synthetic is a single, non-glycosylated, polypeptide chain containing 9 amino acids and having a molecular mass of 1209 Dalton. The molecular formula is C59H84N16O12.

    Formulation

    The Leuprorelin was lyophilized from a concentrated (1mg/ml) solution with no additives.

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    More Info

    • Introduction

      Leuprorelin (INN) or leuprolide acetate (USAN) is a gonadotropin-releasing hormone agonist (GnRH agonist).
      By causing constant stimulation of the pituitaryGnRH receptors, it initially causes stimulation (flare), but thereafter decreases pituitary secretion (downregulation) of gonadotropins luteinizing hormone(LH) and follicle-stimulating hormone(FSH).
      Like other GnRH agonists, leuprolide may be used in the treatment of hormone-responsive cancers such as prostate canceror breast cancer, estrogen-dependent conditions (such as endometriosisor uterine fibroids), to treat precocious puberty, and to control ovarian stimulation in IVF.

    • Synonyms

      Leuprolide, Leuprorelin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      pGlu-His-Trp-Ser-Tyr-D-Leu-Leu-Arg-Pro-NHEt.

    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.

    Leuprolide Human
  • View Data Sheet

    Name :

    b NGF Human, HEK

    Description:

    beta Nerve Growth Factor Human Recombinant, HEK

    Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    Product # :

    CYT-079

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    Description

    BNGF Human Recombinant produced in HEK293 is a noncovalently disulfide linked homodimer, glycosylated, polypeptide chain (Ser122-Arg239) containing 2 identical 118 amino acids and having a molecular mass of 26.5 kDa.

    Source

    HEK293 cells.

    Formulation

    The b-NGF was lyophilized from 1mg/ml in 20mM PB and 0.25M NaCl pH-7.5.

    Purity

    Greater than 97% as obsereved by SDS-PAGE.

    Biological Activity

    The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line), the ED50 is <0.04-0.4ng/ml.

    More Info

    • Introduction

      NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.

    • Synonyms

      Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized b-NGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution b-NGF 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 b-NGF in sterile distilled pyrogen free water at a concentration of 0.25mg/ml.

    • Background

      What is the molecular weight/Mw of B NGF Protein?
      B NGF Protein has a total Mw of 26.5kDa.

      What is the source or expression system of B NGF Protein?
      HEK293 cells.

      What is the Purity of B NGF Protein?

      B NGF Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of B NGF Protein?
      The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line), the ED50 is <0.04-0.4ng/ml.

      What is the amino acid sequence of B NGF Protein?
      B NGF Protein is composed from 118 amino acids.

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

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

    B Ngf Human Hek
  • View Data Sheet

    Name :

    Thyroglobulin Human, Biotin

    Description:

    Thyroglobulin Human, Biotinylated

    Thyroglobulin, TGN, AITD3, TG.

    Product # :

    PRO-2563

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    Description

    Human Thyroglobulin is a biotinylated, glycosylated, polypeptide chain having a total molecular mass of 662 kDa (331 kDa per subunit).

    Source

    Native, Isolated from human thyroid glands.

    Formulation

    Human Thyroglobulin biotinylated is supplied at a 20mM HEPES buffer pH-7.6, 150mM NaCl and 40% Sucrose (w/v).

    Purity

    Greater than 80% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thyroglobulin (TG) represents one of the main autoantigenic targets in autoimmune thyroid disease of humans. TG is a large globular dimeric glycoprotein with a total molecular weight of 660 kDa, which occupies a key precursor role in the biosynthesis of the thyroid hormones. Approximately 75% of the total protein content of the thyroid follicle consists of TG. The thyroid gland uses the Thyroglobulin in order to produce the thyroid hormones thyroxine (T4) and triiodothyronine (T3). Thyroglobulin is produced by the thyroid epithelial cells (thyrocytes) which form spherical follicles. Thyroglobulin is subsequently secreted and stored in the follicular lumen.
      Patients with Hashimoto's thyroiditis or Graves' disease, frequently develop antibodies against Thyroglobulin. Tg-specific antibodies help in the diagnosis of the above diseases, however they also may be present in apparently healthy euthyroid individuals. Blood Thyroglobulin levels can be used as a tumor marker for certain kinds of thyroid cancer, and the may also be elevated in cases of Graves' disease.

    • Synonyms

      Thyroglobulin, TGN, AITD3, TG.

    • Physical Appearance

      Sterile Filtered 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 IgG type human auto antibodies.2. Auto antibodies to thyroglobulin recognize conformation dependent epitopes. 3.Functional Streptavidin based ELISA test (analysis of positive/negative samples.)

    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.

    Thyroglobulin Protein
  • View Data Sheet

    Name :

    LLO

    Description:

    Listeriolysin-O Recombinant

    Listeriolysin-O, LLO, hlyA.

    Product # :

    PRO-320

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    Description

    LLO is a single, non-glycosylated polypeptide chain containing 529 amino acids and having a molecular mass of 58kDa. (accession number: AAF64524).

    Source

    Escherichia Coli.

    Formulation

    The protein contains 50mM NaH2PO4, 1mM EDTA, 2.7mM KCl, pH 6.4, 1mM DTT, 5% (v/v) glycerol and 0.5M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    Hemolytic activity is 8,27E+05  HU/mg of protein where HU means hemolytic activity unit that is the amount of toxin needed to release half the hemoglobin (50% lysis) of the erythrocytes as determined by hemolysin assay.

    More Info

    • Introduction

      Listeriolysin O (aka LLO) is a hemolysin produced by Listeria monocytogenes bacteria, the pathogen responsible for causing listeriosis. The toxin may be regarded as a virulence factor, since it is crucial for the virulence of L. monocytogenes. LLO is a single polypeptide protein encoded by the hlyA gene and composed of 529 residues. LLO is a thiol-activated cholesterol-dependent pore forming toxin protein; therefore, it is activated by reducing agents and inhibited by oxidizing agents. Still, LLO differs from other thiol-activated toxins, as its cytolytic activity is maximized at a pH of 5.5. Inside the acidic phagosomes (average pH ~ 5.9) of cells that have phagocytosed L. monocytogenes, LLO is selectively activated by maximizing activity at a pH of 5.5. Following the phagosome lysis by LLO, the bacterium breaks out into the cytosol, where it is able to grow intracellularly, and the toxin has reduced activity in the more basic cytosol. Thus, LLO permits L. monocytogenes to break out from the phagosomes into the cytosol without harming the plasma membrane of the infected cell, which allows the bacteria to live intracellularly, where they are sheltered from extracellular immune system factors such as the complement system and antibodies. LLO also brings about dephosphorylation of histone H3 and deacetylation of histone H4 in the early phases of infection, before entry of L. monocytogenes into the host cell. The pore-forming activity is not implicated in causing the histone modifications. The modifications of the histones affect the down regulation of genes encoding proteins involved in the inflammatory response. Therefore, LLO may be significant in subverting the host immune response to L. monocytogenes. At its NH2-terminus it possesses a 25 residues long typical signal sequence excited during the secretion process. Moreover, in its NH2-terminus there is also a 19 amino acids PEST- like sequence that may target this toxin for degradation. The PEST-like sequence found in LLO and is considered crucial for virulence, given that mutants lacking the sequence lysed the host cell. Nevertheless, contrary to PEST's supposed role in protein degradation, evidence implies that the PEST-like sequence may control LLO production in the cytosol rather than increase degradation of LLO.

    • Synonyms

      Listeriolysin-O, LLO, hlyA.

    • 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.

    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.

    Listeriolysin O
  • View Data Sheet

    Name :

    sRANKL Human, His

    Description:

    Soluble RANK Ligand Human Recombinant, His Tag

    Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

    Product # :

    CYT-692

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    Description

    sRANKL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids (140-317 a.a) and having a molecular mass of 22.3kDa.sRANKL is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    sRANKL protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RANKL binds to tnfrsf11b/opg and to tnfrsf11a/rank. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive t-cell proliferation. May be an important regulator of interactions between t-cells and dendritic cells and may play a role in the regulation of the t-cell-dependent immune response. sRANKL may also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy.

    • Synonyms

      Soluble Receptor Activator of NFkB Ligand, TNFSF11, TRANCE, TNF-related activation-induced cytokine, OPGL, ODF, Osteoclast differentiation factor, Tumor necrosis factor ligand superfamily member 11, Receptor activator of nuclear factor kappa B ligand, RANKL, Osteoprotegerin ligand, CD254 antigen, sRANKL, sOdf, hRANKL2.

    • 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 MIRAEKAMVD GSWLDLAKRS KLEAQPFAHL TINATDIPSG SHKVSLSSWY HDRGWAKISN MTFSNGKLIV NQDGFYYLYA NICFRHHETS GDLATEYLQL MVYVTKTSIK IPSSHTLMKG GSTKYWSGNS EFHFYSINVG GFFKLRSGEE ISIEVSNPSL LDPDQDATYF GAFKVRDID.

    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.

    Srankl Human His
  • View Data Sheet

    Name :

    Der F1

    Description:

    Der F1 Mosaic Protein Recombinant

    Product # :

    ALR-004

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    Description

    The E.Coli derived recombinant protein contains the Dermatophagoides farina Der F1 full length protein (a.a. 1-320) and fused to a 6 His Tag at C-terminus, having a total Mw of 36kDa, pI 5.88.

    Source

    E.Coli.

    Formulation

    60mM NaCl, 50mM Tris-HCl pH 8.0 and 1.2M Urea.

    Purity

    Protein is >95% pure as determined by 10% PAGE (coomassie staining) and RP-HPLC.

    More Info

    • Introduction

      DERF1 is a thiol protease that hydrolyzes proteins, with a preference for Phe or basic residues. DERF1 is a C1 peptidase family member. DERF1 has extensive endopeptidase specificity. DERF1 causes an allergic reaction in humans. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Der F1 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Purification Method

      Purified by proprietary chromatographic technique.

    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.

    Der F1
  • View Data Sheet

    Name :

    TNNI3 Human Native

    Description:

    Cardiac Troponin-I Human

    Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    Product # :

    PRO-2788

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    Description

    TNNI3 Native produced in Human heart tissue is a full length protein which has an additional amino acid residues on its N terminus that are not present on the skeletal form, making this protein a promising analyte for indicating cardiac specificity.TNNI3 Native is purified by proprietary chromatographic technique.

    Source

    Human heart tissue.

    Formulation

    TNNI3 was lyophilized from 0.01M HCl.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Troponin I cardiac muscle, Cardiac troponin I, TNNI3, TNNC1, CMH7, RCM1, cTnI, CMD2A, MGC116817.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Cardiac Troponin-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI3 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 TNNI3 in Tris/urea buffer (20mM Tris, pH 7.5, 7M urea, 5mM EDTA, 15mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Troponin I, encoded by the TNNI3 gene, is a critical component of the troponin complex in cardiac muscle cells. It plays a central role in the regulation of cardiac muscle contraction by modulating the interaction between actin and myosin filaments.

      While extensive research has been conducted on troponin I in the context of cardiac diseases, there is a growing need to investigate native human troponin I (TNNI3) in its unmodified form to gain a deeper understanding of its functions, structural significance, and implications for heart health. This research aims to provide a comprehensive exploration of TNNI3 in its native state, shedding light on its various roles and potential applications in cardiology and biomedical research.

      The primary objective of this research is to elucidate the physiological role of native human TNNI3 in cardiac muscle contraction. Experiments involving human cardiac tissue samples and isolated myocytes will be conducted to investigate how TNNI3 interacts with other components of the troponin complex and influences calcium-mediated muscle contraction. Understanding these mechanisms is fundamental for deciphering the complexities of cardiac muscle physiology and its implications for heart health.

      The second objective is to assess the clinical relevance of native TNNI3 in cardiac diseases. Clinical studies involving patients with various cardiac conditions will be conducted to evaluate the diagnostic and prognostic value of TNNI3 as a biomarker. These investigations may provide valuable insights into the use of native TNNI3 in the early detection and management of heart diseases.

      The third objective is to explore the potential applications of native TNNI3 in biomedical research and drug development. Research will investigate the use of native TNNI3-expressing cells as models for studying cardiac disorders and for developing novel therapeutic interventions targeting the troponin complex.

      By delving into the functions and roles of native human TNNI3, this research aims to expand our knowledge of cardiac muscle physiology, its implications for cardiac diseases, and its potential applications in cardiology and biomedical research.

    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.

    Cardiac Troponin 1 2
  • View Data Sheet

    Name :

    GLP1R Human

    Description:

    Glucagon Like Peptide 1 Receptor Human Recombinant

    GLP1, GLP2, GRPP

    Product # :

    HOR-027

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    Description

    GLP1R Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 24-145) containing 132 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 15.55 kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    GLP1R filtered (0.4 µm) and lyophilized from 0.5mg/ml in 50mM Acetate Buffer, pH 4.0.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The glucagon-like peptide-1 receptor, also known as GLP1R, is a receptor protein found on brain neurons and beta cells of the pancreas. GLP1R activates a signalling cascade that leads to the initiation of adenylyl cyclase and increased intracellular cAMP levels. In humans, GLP1R is synthesized by GLP1R gene, which is present on chromosome 6.
      GLP1R takes part in the control of blood sugar level by enhancing insulin secretion. GLP1R is a part of the glucagon receptor family of G protein-coupled receptors. GLP1R consists of two domains, one transmembrane (TMD) domain, that binds the N-terminal region of GLP-1. And one extracellular (ECD) which binds the C-terminal helix of GLP-1. The TMD domain contains a fulcrum of polar residues that controls the biased signaling of the receptor, while the transmembrane helical boundaries and extracellular surface are a trigger for biased agonism.

    • Synonyms

      GLP1, GLP2, GRPP

    • 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 reconstitute the lyophilized Hepatocyte Growth Factor in 100mM Acetate buffer to a working concentration approximately 0.5mg/ml. Further dilutions should be made using buffer containing protein.

    • Amino Acid Sequence

      MKHHHHHHAS RPQGATVSLW ETVQKWREYR RQCQRSLTED PPPATDLFCN RTFDEYACWP DGEPGSFVNV SCPWYLPWAS SVPQGHVYRF CTAEGLWLQK DNSSLPWRDL SECEESKRGE RSSPEEQLLF LY

    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.

    Glp1R Human
  • View Data Sheet

    Name :

    LGALS9 Mouse

    Description:

    Galectin-9 Mouse Recombinant

    Galectin-9, Gal-9, Lgals9, Lgals5, LGALS35, AA407335, AI194909, AI265545.

    Product # :

    CYT-550

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    • SDS-PAGE

    Description

    LGALS9 mouse Recombinant produced E. coli is a single polypeptide chain containing 345 amino acids (1-322) and having a molecular mass of 38kDa.LGALS9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LGALS9 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    LGALS9 Mouse-SDS-PAGE - Product image 1

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    • Introduction

      LGLAS9 binds galactosides and has high affinity for the Forssman pentasaccharide. LGLAS9 participates in thymocyte-epithelial interactions relevant to the biology of the thymus and Inhibits cell proliferation. LGLAS9 is a ligand for HAVCR2/TIM3. LGLAS9 Induces T-helper type 1 lymphocyte (Th1) death. LGLAS9 performs as an eosinophil chemoattractant LGLAS9 is an S-type lectin which is over-expressed in Hodgkin's disease tissue and takes part in the interaction between the H&RS cells with their surrounding cells.

    • Synonyms

      Galectin-9, Gal-9, Lgals9, Lgals5, LGALS35, AA407335, AI194909, AI265545.

    • 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 MGSMALFSAQ SPYINPIIPF TGPIQGGLQE GLQVTLQGTT KSFAQRFVVN FQNSFNGNDI AFHFNPRFEE GGYVVCNTKQ NGQWGPEERK MQMPFQKGMP FELCFLVQRS EFKVMVNKKF FVQYQHRVPY HLVDTIAVSG CLKLSFITFQ TQNFRPAHQA PMAQTTIHMV HSTPGQMFST PGIPPVVYPT PAYTIPFYTP IPNGLYPSKS IMISGNVLPD ATRFHINLRC GGDIAFHLNP RFNENAVVRN TQINNSWGQE ERSLLGRMPF SRGQSFSVWI ICEGHCFKVA VNGQHMCEYY HRLKNLQDIN TLEVAGDIQL THVQT.

    • Background

      What is the molecular weight/Mw of LGALS9 MOUSE Protein?
      LGALS9 MOUSE Protein has a total Mw of 38kDa.

      What is the source or expression system of LGALS9 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of LGALS9 MOUSE Protein?
      LGALS9 MOUSE Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS9 MOUSE Protein?
      The biological functionality of LGALS9 MOUSE Protein will be determined in the future.

      What is the amino acid sequence of LGALS9 MOUSE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMALFSAQ SPYINPIIPF TGPIQGGLQE GLQVTLQGTT KSFAQRFVVN FQNSFNGNDI AFHFNPRFEE GGYVVCNTKQ NGQWGPEERK MQMPFQKGMP FELCFLVQRS EFKVMVNKKF FVQYQHRVPY HLVDTIAVSG CLKLSFITFQ TQNFRPAHQA PMAQTTIHMV HSTPGQMFST PGIPPVVYPT PAYTIPFYTP IPNGLYPSKS IMISGNVLPD ATRFHINLRC GGDIAFHLNP RFNENAVVRN TQINNSWGQE ERSLLGRMPF SRGQSFSVWI ICEGHCFKVA VNGQHMCEYY HRLKNLQDIN TLEVAGDIQL THVQT.
      What applications can LGALS9 MOUSE Protein be used in?
      LGALS9 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS9 MOUSE Protein?
      The endotoxin level is minimal, LGALS9 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.

    Lgals9 Mouse
  • View Data Sheet

    Name :

    Activin A Human

    Description:

    Activin A Human Recombinant

    Activin Beta-A chain, Erythroid differentiation protein, EDF, FRP, Activin-A, Inhibin-B, Inihibin-Beta A chain.

    Product # :

    CYT-569

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • sds-page

    Description

    Activin-A Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 137 amino acids (311-426) and having a molecular mass of 15.2kDa.Activin-A is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Activin-A protein solution (1mg/ml) contains 20mM Tris pH 8.0 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    Activin A Human sds-page - Product image 1

    More Info

    • Introduction

      Inhibins are dimeric peptide hormones produced by female ovarian granulose cells and male Sertoli cells as well as a variety of other tissues. Inhibins have two isoforms, A and B, with the same alpha subunit but different beta subunits. Inhibin A is a dimer of alpha and beta A subunits, inhibin B is a dimer of alpha and beta B subunits.
      Inhibins are thought to inhibit the production of follicle-stimulating hormone (FSH) by the pituitary gland. In addition, Inhibins are also thought to play a role in the control of gametogenesis, and embryonic and fetal development.

    • Synonyms

      Activin Beta-A chain, Erythroid differentiation protein, EDF, FRP, Activin-A, Inhibin-B, Inihibin-Beta A chain.

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

    • Background

      What is the molecular weight / Mw of Activin A Protein?
      Activin A Protein has a total Mw of 15.2 kDa.

      What is the source or expression system of Activin A Protein?
      E.Coli

      What is the Purity of Activin A Protein?
      Activin A Protein is >90% 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?MGSSHHHHHH SSGLVPRGSH MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS

      What applications can ACTIVIN-A Protein be used in?

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

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

    Activin A Human
  • View Data Sheet

    Name :

    CXCL7 Human

    Description:

    Neutrophil Activating Protein-2 Human 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-274

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
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    • More Info

    Description

    Neutrophil Activating Protein-2 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 70 amino acids and having a molecular mass of 7609 Dalton. The NAP-2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CXCL7 protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.

    Purity

    Greater than 97% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/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 CXCL7should 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 Neutrophil Activating Protein-2in 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 Ala-Glu-Leu-Arg-Cys.

    • Background

      What is the molecular weight/Mw of CXCL7 HUMAN Protein?
      CXCL7 HUMAN Protein has a total Mw of 7.6kDa.

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

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

      What is the Biological Activity of CXCL7 HUMAN Protein?
      The specific activity as determined by the ability of NAP2 to chemoattract human neurotrophils using a concentration of 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of CXCL7 HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Glu-Leu-Arg-Cys.

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

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

    Nap2 Human
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