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Search results

1000 results found for “ephrin”

Name

Description

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  • View Data Sheet

    Name :

    Buserelin

    Description:

    Buserelin

    Product # :

    HOR-255

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    Description

    Buserelin contains 9 amino acids Glu-His-Trp-Ser-Tyr-D-Ser(tBu)-Leu-Arg-Pro-NHEt and having a molecular weight of 1239.44 Dalton.

    Formulation

    The Buserelin 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

      Buserelin belongs to the group of gonadotrophin releasing hormone (gonadorelin) analogues (LHRH agonist). It acts on the pituitary gland which controls the amount of many different types of hormones (chemical messengers). It alters the amount of hormones, particularly the oestrogens androgens. This alteration of hormone levels can be exploited to treat cancers of the prostate gland, which are stimulated to grow by testosterone. Buserelin lowers the levels of testosterone, which starves the tumour of testosterone and causes it to shrink.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Buserelin
  • View Data Sheet

    Name :

    ACVR1 Human

    Description:

    Activin A Receptor Type 1 Human Recombinant

    ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.

    Product # :

    CYT-1140

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    • More Info
    • sds-page

    Description

    ACVR1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 342 amino acids (21-123a.a.) and having a molecular mass of 38.4kDa. ACVR1 is expressed with a 239 amino acid hIgG-His-Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    ACVR1 protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    sds-page

    ACVR1 Human sds-page - Product image 1

    More Info

    • Introduction

      Activin A Receptor Type 1 (ACVR1) is a member of TGF-beta serine/threonine kinase receptor family. ACVR1 forms a receptor complex contains2 type II and 2 type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate,bind and activate SMAD transcriptional regulators. ACVR1 takes part in left-right pattern formation during embryogenesis and is also essential in the BMP pathway which is responsible for the development and repair of the skeletal system.ACVR1 is linked to Fibrodysplasia Ossificans Progressiva which isknown for the formation of heterotopic bone throughout the body.

    • Synonyms

      ACVR1A, ALK2, ACVR1, ACTRI, ACTR-I, ACVRLK2, FOP, SKR1, TSRI, Activin receptor type I, Activin receptor-like kinase 2, ALK-2, TSR-I, Serine/threonine-protein kinase receptor R1, TGF-B superfamily receptor type I.

    • 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

      MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
      CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
      PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
      REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
      PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
      VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

    • Background

      Functional Implications and Therapeutic Prospects of Activin A Receptor Type 1 Human Recombinant

      1. Abstract

      This study illuminates the functional roles and potential therapeutic applications of Activin A Receptor Type 1 Human Recombinant (ACVR1), a crucial protein in the TGF-beta superfamily signaling pathway. Through a comprehensive review of its structure, signaling mechanism, biological functions, and disease associations, this paper aims to elucidate the current understanding of ACVR1 and its potential therapeutic implications in various disease states.

      2. Introduction

      The Activin A Receptor Type 1 Human Recombinant, abbreviated as ACVR1, is a receptor protein vital for transmitting cellular signals in the Transforming Growth Factor-beta (TGF-beta) superfamily pathway. Known to play pivotal roles in organogenesis, bone growth, and cell differentiation, the ACVR1 and its functions present vast therapeutic potential.

      3. Structure and Signaling of ACVR1

      ACVR1 is a transmembrane serine/threonine kinase receptor, characterized by an extracellular ligand-binding domain and an intracellular kinase domain for signal transduction. Binding of ligands such as Activin A leads to the formation of heteromeric complexes with type II receptors, triggering phosphorylation events that activate downstream signaling pathways.

      4. Biological Functions of ACVR1

      Being a part of the TGF-beta superfamily signaling pathway, ACVR1 is implicated in a broad spectrum of biological processes. It is crucial for embryonic development, cellular proliferation, differentiation, apoptosis, and homeostasis. It also plays a significant role in bone morphogenesis, contributing to skeletal patterning and growth.

      5. ACVR1 in Disease Pathology

      The dysregulation of ACVR1 has been associated with various pathological conditions, including Fibrodysplasia Ossificans Progressiva (FOP), a rare genetic disorder characterized by progressive ossification of soft tissues. Mutations in ACVR1 lead to enhanced BMP signaling, causing aberrant bone formation. This highlights the critical role of ACVR1 in skeletal homeostasis and disease.

      6. Therapeutic Potential of ACVR1

      Given the central role of ACVR1 in cellular signaling and its association with disease, it presents a promising target for therapeutic intervention. Strategies to modulate ACVR1 signaling could potentially ameliorate symptoms of diseases like FOP, offering promising avenues for novel therapeutic approaches.

      7. Conclusion and Future Perspectives

      While our understanding of ACVR1's functional roles has expanded significantly over the years, much remains to be elucidated. Further research into the precise molecular mechanisms of ACVR1 and its pathway will pave the way for therapeutic advances, enhancing our capability to combat various diseases.

      What is the molecular weight / Mw of ACVR1 Protein?
      ACVR1 Protein has a total Mw of 38.4kDa.

      What is the source or expression system of ACVR1 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of ACVR1 Protein?
      ACVR1 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of ACVR1 Protein?
      The biological functionality of ACVR1 Protein will be determined in the future.

      What is the endotoxin level for ACVR1 Protein?
      The endotoxin level is minimal, ACVR1 Protein was purified using conventional chromatography techniques.

      What is the amino acid sequence of ACVR1 Protein?
      MEDEKPKVNP KLYMCVCEGL SCGNEDHCEG QQCFSSLSIN DGFHVYQKGC FQVYEQGKMT
      CKTPPSPGQA VECCQGDWCN RNITAQLPTK GKSFPGTQNF HLELEPKSCD KTHTCPPCPA
      PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP
      REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL
      PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT
      VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

      What applications can ACVR1 Protein be used in?
      ACVR1 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.

    Acvr1 Human
  • View Data Sheet

    Name :

    EEF1B2 Human

    Description:

    Eukaryotic Translation Elongation Factor 1 Beta 2 Human Recombinant

    Elongation factor 1-beta, EF-1-beta, EEF1B2, EEF1B, EF1B, EEF1B1.

    Product # :

    PRO-167

    Price :

    Quantity :

    Shipping Method :

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    • description
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    • More Info

    Description

    EEF1B2 Human Recombinant fused with an 8 amino acid His tag at C-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 233 amino acids (1-225 a.a.) and having a molecular mass of 25.8kDa. The EEF1B2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The EEF1B2 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 1mM DTT and 100mM NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Elongation factor 1-beta (EEF1B2) is a translation elongation factor. EEF1B2 is a guanine nucleotide exchange factor which is involved in the transfer of aminoacylated tRNAs to the ribosome. Both EEF1B2 and EEF1D stimulate the exchange of GDP bound to EEF1A to GTP.

    • Synonyms

      Elongation factor 1-beta, EF-1-beta, EEF1B2, EEF1B, EF1B, EEF1B1.

    • 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

      MGFGDLKSPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSSPPPADLC HALRWYNHIK SYEKEKASLP GVKKALGKYG PADVEDTTGS GATDSKDDDD IDLFGSDDEE ESEEAKRLRE ERLAQYESKK AKKPALVAKS SILLDVKPWD DETDMAKLEE CVRSIQADGL VWGSSKLVPV GYGIKKLQIQ CVVEDDKVGT DMLEEQITAF EDYVQSMDVA AFNKILEHHH HHH.

    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.

    Eef1B2 Human
  • View Data Sheet

    Name :

    EGF Antibody

    Description:

    Endothelial Growth Factor, Mouse Anti-Human

    Urogastrone, URG, EGF.

    Product # :

    ANT-169

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

    Add To Cart

    More Info

    • formulation
    • More Info

    Formulation

    1mg/ml in PBS (after reconstitution).

    More Info

    • Introduction

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

    • Synonyms

      Urogastrone, URG, EGF.

    • Solubility

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

    • Immunogen

      r.HumanEGF.

    • Ig Subclass

      Mouse IgG2b.

    • Clone

      NYRhEGF.

    • Applications

      Direct ELISA, Western Blot, Immuneprecipitation.

    • Titer

      By direct ELISA, 1:10,000 dilution will yield 0.3 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).

    • Shipping Conditions

      Antibody is shipped lyophilized at ambient temperature.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      In lyophilized form, for long periods, store at 4oC in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20oC.

    • Purification Method

      Ion exchange.

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

    Egf Antibody
  • View Data Sheet

    Name :

    Fibronectin Rat

    Description:

    Fibronectin Rat

    Product # :

    PRO-131

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    Description

    Plasma fibronectin level is elevated in severe coronary artery disease. Increased plasma fibronectin levels are related with venous thromboembolism (VTE) particularly in males, and extend the probable association between biomarkers and risk factors for arterial atherothrombosis and VTE. Fibronectin plays a role in several cellular processes, including tissue repair, embryogenesis, blood clotting, and cell migration/adhesion. Fibronectin consists in two main forms: 1) as an insoluble glycoprotein dimer that serves as a linker in the etracellular matrix and 2) as a soluble disulphide linked dimer found in the plasma. The plasma form is produced by hepatocytes, and the ECM form is synthesized by fibroblasts, chondrocytes, endothelial cells, macrophages, as well as certain epithelial cells. Fibronectin alos takes part as a general cell adhesion molecule by anchoring cells to collagen or proteoglycan substrates. Fibronectin organizes cellular interaction with the ECM by binding to different components of the extracellular matrix and to membrane-bound Fibronectin receptors on cell surfaces. Molecular Weight 220kDa.

    Source

    Rat Plasma.

    Formulation

    The Rat Fibronectin was lyophilized from a concentrated 1mg/ml solution containing 20mM Tris Cl pH-7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized fibronectin at 4°C. Upon reconstitution fibronectin should be stored at 4°C for 2 weeks and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

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

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

    Fibronectin Rat
  • View Data Sheet

    Name :

    Follistatin Human

    Description:

    Follistatin Human Recombinant

    FST, FS

    Product # :

    CYT-232

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    • source
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    Description

    Follistatin Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 288 amino acids and having a total molecular mass of 31.5kDa.The FST is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing no additives.

    Purity

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

    Biological Activity

    The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.

    More Info

    • Introduction

      Follistatin is a single-chain gonadal protein that specifically inhibits follicle-stimulating hormone release. The single FST gene encodes two isoforms, FST317 and FST344 containing 317 and 344 amino acids respectively, resulting from alternative splicing of the precursor mRNA. In a study in which 37 candidate genes were tested for linkage and association with polycystic ovary syndrome (PCOS) or hyperandrogenemia in 150 families, evidence was found for linkage between PCOS and follistatin. Follistatin functions as an ACTV antagonist. specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (fsh).

    • Synonyms

      FST, FS

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Follistatin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution FST 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 Follistatin 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 Gly-Asn-Cys-Trp-Leu.

    • Background

      What is the molecular weight/Mw of FOLLISTATIN HUMAN Protein?
      FOLLISTATIN HUMAN Protein has a total Mw of 31.5kDa.

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

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

      What is the Biological Activity of FOLLISTATIN HUMAN Protein?
      The activity is determined by the ability to neutralize ACTV inhibitory effect of mouse MPC-11 cells. The expected ED50 is 100-400ng/ml, corresponding to a Specific Activity of 2,500-10,000units/mg in the presence of 7.5ng/ml ACTV A.

      What is the amino acid sequence of FOLLISTATIN HUMAN Protein?
      The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Asn-Cys-Trp-Leu.

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

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

    Follistatin Human
  • View Data Sheet

    Name :

    Adiponectin Human, HMW

    Description:

    Adiponectin glycosylated Human Recombinant, HMW Rich

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

    Product # :

    CYT-764

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    Description

    Adiponectin Human Recombinant HMW Rich produced in HEK cells is a single, glycosylated, polypeptide chain (19-244) containing a total of 226 amino acids, having a molecular mass of 24.6kDa (calculated). Human Acrp30 HMW Rich migrates on SDS-PAGE under non-reducing conditions at ~ 884 kDa.

    Source

    HEK293.

    Formulation

    Acrp30 was filtered (0.4µm) and lyophilized from 0.5mg/ml in 20mM Tris, 50mM NaCl, pH 7.5 and 1mM CaCl2.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Adiponectin is a recently discovered 244 amino acid protein, the product of the apM1 gene, which is physiologically active and specifically and highly expressed in adipose cells (Adipokine). The protein belongs to the soluble defense collagen super family; it has a collagen-like domain structurally homologous with collagen VIII and X and complement factor C1q-like globular domain. APM-1 forms homotrimers, which are the building blocks for higher order complexes found circulating in serum.

    • Synonyms

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

    • 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.

    • Solubility

      It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Acrp30 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.

    • Background

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

      What is the source or expression system of ADIPONECTIN Protein?
      HEK293.


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

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

      What is the amino acid sequence of ADIPONECTIN Protein?
      ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHITVYM KDVKVSLFKK DKAMLFTYDQ YQENNVDQAS GSVLLHLEVG DQVWLQVYGE GERNGLYADN DNDSTFTGFL LYHDTN.

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

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

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

    Adiponectin Human Hmw
  • View Data Sheet

    Name :

    Resistin Mutant Human

    Description:

    Resistin Mutant Human Recombinant

    Resistin, Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-585

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    Description

    9.9 kDa protein containing 93 amino acid residues, produced in E.coli. Mutant-Resistin has had a Cysteine residue mutated to prevent dimerization and possibly acts as an antagonist.

    Source

    Escherichia Coli.

    Formulation

    Recombinant Human Resistin was lyophilized from a concentrated (1mg/ml) solution containing 0.1% TFA.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrophobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
      Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severely suppressed in obesity and is stimulated by several antidiabetic drugs.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Resistin, Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • 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 0.2 ml of deionized water and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MSSKTLCSME EAINERIQEV AGSLIFRAIS SIGLECQSVT SRGDLATCPR GFAVTGCTCG SACGSWDVRA ETTCHCQCAG MDWTGARCCR VQP.

    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.

    Resistin Mutant Human
  • View Data Sheet

    Name :

    PFN4 Human

    Description:

    Profilin-4 Human Recombinant

    PFN-4, Profilin-IV, Profilin4.

    Product # :

    PRO-818

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    Description

    PFN4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 149 amino acids (1-129 a.a.) and having a molecular mass of 16.4 kDa. PFN4 protein is fused to a 20 amino acid His tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    PFN4 Human solution containing 20mM Trsi HCL pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      PFN4 is a small actin-binding protein that participates in the dynamic turnover and restructuring of the actin cytoskeleton. PFN4 is localized in all eukaryotic organisms in the majority of cells. PFN4 is crucial for spatially and temporally controlled growth of actin microfilaments, which is a necessary process in cellular locomotion and cell shape changes.

    • Synonyms

      PFN-4, Profilin-IV, Profilin4.

    • 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 MSHLQSLLLD TLLGTKHVDS AALIKIQERS LCVASPGFNV TPSDVRTLVN GFAKNPLQAR REGLYFKGKD YRCVRADEYS LYAKNENTGV VVVKTHLYLL VATYTEGMYP SICVEATESL GDYLRKKGS.

    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.

    Pfn4 Human
  • View Data Sheet

    Name :

    PHB2 Human

    Description:

    Prohibitin 2 Human Recombinant

    BAP, Bap37, BCAP37, p22, PNAS-141, REA, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity, PHB2.

    Product # :

    PRO-1533

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    Description

    PHB2 Human Recombinant produced in E. coli is a single polypeptide chain containing 322 amino acids (1-299) and having a molecular mass of 35.7kDa. PHB2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PHB2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Prohibitin 2, also known as PHB2, mediates transcriptional repression by nuclear hormone receptors via recruitment of histone deacetylases by similarity. PHB2 functions as an estrogen receptor (ER)-selective coregulator which potentiates the inhibitory activities of antiestrogens and represses the activity of estrogens. PHB2 which is involved in regulating mitochondrial respiration activity and in aging, competes with NCOA1 for modulation of ER transcriptional activity.

    • Synonyms

      BAP, Bap37, BCAP37, p22, PNAS-141, REA, Prohibitin-2, B-cell receptor-associated protein BAP37, D-prohibitin, Repressor of estrogen receptor activity, PHB2.

    • 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 MGSMAQNLKD LAGRLPAGPR GMGTALKLLL GAGAVAYGVR ESVFTVEGGH RAIFFNRIGG VQQDTILAEG LHFRIPWFQY PIIYDIRARP RKISSPTGSK DLQMVNISLR VLSRPNAQEL PSMYQRLGLD YEERVLPSIV NEVLKSVVAK FNASQLITQR AQVSLLIRRE LTERAKDFSL ILDDVAITEL SFSREYTAAV EAKQVAQQEA QRAQFLVEKA KQEQRQKIVQ AEGEAEAAKM LGEALSKNPG YIKLRKIRAA QNISKTIATS QNRIYLTADN LVLNLQDESF TRGSDSLIKG KK.

    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.

    Phb2 Human
  • View Data Sheet

    Name :

    Eotaxin Rat

    Description:

    Eotaxin Rat Recombinant (CCL11)

    Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.

    Product # :

    CHM-260

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    • description
    • source
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    Description

    Eotaxin Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 74 amino acids and having a molecular mass of 8.4kDa. The CCL11 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Filtered (0.2µm) and lyophilized from a concentrated (1mg/ml) solution in in 1×PBS, pH7.4.

    Purity

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

    Biological Activity

    Determined by its ability to chemoattract purified blood eosinophils using a concentration range of 0.1-1.0 ug/ml, corresponding to a Specific Activity of 10-100IU/mg.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 11 (CCL11) is a small cytokine belonging to the CC chemokine family that is also known as eotaxin. CCL11 selectively recruits eosinophils by inducing their chemotaxis, and therefore, is implicated in allergic responses. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for which CCL11 is a ligand include CCR2, CCR3 and CCR5. The gene for human CCL11 (scya11) is encoded on three exons and is located on chromosome 17.

    • Synonyms

      Small inducible cytokine A11, CCL11, Eosinophil chemotactic protein, chemokine (C-C motif) ligand 11, SCYA11.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Eotaxin although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution CCL11 should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      HPGSIPTSCC FTMTSKKIPN TLLKSYKRIT NNRCTLKAIV FKTKLGKEICADPKKKWVQD ATKHLDQKLQ TPKP.

    • Background

      What is the molecular weight/Mw of EOTAXIN RAT Protein?
      EOTAXIN RAT Protein has a total Mw of 8.4kDa.

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

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

      What is the Biological Activity of EOTAXIN RAT Protein?
      Determined by its ability to chemoattract purified blood eosinophils using a concentration range of 0.1-1.0 ug/ml, corresponding to a Specific Activity of 10-100IU/mg.

      What is the amino acid sequence of EOTAXIN RAT Protein?
      HPGSIPTSCC FTMTSKKIPN TLLKSYKRIT NNRCTLKAIV FKTKLGKEICADPKKKWVQD ATKHLDQKLQ TPKP.

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

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

    Eotaxin Rat
  • View Data Sheet

    Name :

    ETNK2 Human

    Description:

    EthanolamineKinase 2 Human Recombinant

    Ethanolaminekinase-2

    Product # :

    PKA-077

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    Description

    ETNK2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 409 amino acids (1-386 a.a) and having a molecular mass of 47.2kDa.ETNK2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ETNK2 protein solution (0.25mg/ml) in Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ETNK2 belongs to theethanolaminekinase family which catalyzes the 1st step of PtdEtn biosynthesis via the cytidine diphosphate.

    • 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 MGSMAVPPSA PQPRASFHLR RHTPCPQCSW GMEEKAAASA SCREPPGPPR AAAVAYFGIS VDPDDILPGA LRLIQELRPH WKPEQVRTKR FTDGITNKLV ACYVEEDMQD CVLVRVYGER TELLVDRENE VRNFQLLRAH SCAPKLYCTF QNGLCYEYMQ GVALEPEHIR EPRLFRLIAL EMAKIHTIHA NGSLPKPILW HKMHNYFTLV KNEINPSLSA DVPKVEVLER ELAWLKEHLS QLESPVVFCH NDLLCKNIIY DSIKGHVRFI DYEYAGYNYQ AFDIGNHFNE FAGVNEVDYC LYPARETQLQ WLHYYLQAQK GMAVTPREVQ RLYVQVNKFA LASHFFWALW ALIQNQYSTI DFDFLRYAVI RFNQYFKVKP QASALEMPK.

    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.

    Etnk2 Human
  • View Data Sheet

    Name :

    PEDF PAT13D9AT Antibody

    Description:

    Mouse Anti Human Pigment Epithelium-Derived Factor Clone PAT13D9AT

    Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    Product # :

    ANT-714

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    • More Info

    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

    More Info

    • Introduction

      PEDF is a noninhibitory serpin with neurotrophic, anti-angiogenic, and anti-tumorigenic properties. PEDF is a 50,000 dalton glycoprotein created and secreted in many tissues all the way through the body. A key component of the anti-angiogenic action of PEDF is the induction of apoptosis in proliferating endothelial cells. Additionally, PEDF is capable to inhibit the activity of angiogenic factors such as VEGF and FGF-2. The neuro-protective effects of PEDF are achieved through suppression of neuronal apoptosis induced by peroxide, glutamate, or other neurotoxins. The recognition of a lipase-linked cell membrane receptor for PEDF (PEDF-R) that binds to PEDF with high affinity should facilitate further elucidation of the underlying mechanisms of this pluripotent serpin. To date, PEDF-R is the only signaling receptor known to be used by a serpin family member. The unique range of PEDF activities associate it as a potential therapeutic agent for the treatment of vasculature related neurodegenerative diseases such as age-related macular degeneration (AMD) and proliferative diabetic retinopathy (PDR). PEDF in addition has the potential to be functional in the treatment of various angiogenesis-related diseases including a number of cancers.

    • Synonyms

      Pigment epithelium-derived factor,PEDF, Serpin-F1, SerpinF1, EPC-1, EPC1, PIG35.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human PEDF mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human PEDF protein 20-418 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG1 heavy chain and κ light chain.

    • Clone

      PAT13D9AT.

    • Applications

      PEDF antibody has been tested by ELISA, Western blot analysis and ICC/IF to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      PEDF antibody was purified by protein-A affinity chromatography.

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

    Pedf Pat13D9At Antibody
  • View Data Sheet

    Name :

    EGF Human, Pichia

    Description:

    Epidermal Growth Factor Human Recombinant, Pichia

    Urogastrone, URG, EGF.

    Product # :

    CYT-332

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    Description

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

    Source

    Pichia Pastoris.

    Formulation

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

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

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

    • Synonyms

      Urogastrone, URG, EGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Epidermal Growth Factor Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW E.

    • Background

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

      Abstract:

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

      Introduction:

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

      Pichia as an Expression Host:

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

      Genetic Engineering Strategies:

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

      Fermentation and Protein Purification:

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

      Bioinformatics in EGF-Pichia Interaction:

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

      Therapeutic Implications:

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

      Challenges and Future Directions:

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

      Conclusion:

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

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

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

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

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

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

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

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

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

    Egf Human Pichia
  • View Data Sheet

    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 :

    EDAR Antibody

    Description:

    Ectodysplasin A Receptor, Mouse Anti Human

    Ectodysplasin A Receptor, DL, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Ectodysplasin-A Receptor, Downless Homolog, EDA-A1 Receptor, ECTD10A, ECTD10B, EDA3, HRM1, ED3, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, EDA-A1R, EDA1R, ED1R, ED5, Tumor necrosis factor receptor superfamily member EDAR.

    Product # :

    ANT-560

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    Formulation

    1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.

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    • Introduction

      Ectodysplasin A Receptor, also known as EDAR belongs to the tumor necrosis factor receptor family. EDAR is a receptor for the soluble ligand ectodysplasin A, and is capable of activating the nuclear factor-kappaB, JNK, as well as caspase-independent cell death pathways. EDAR is necessary for the development of hair, teeth, and other ectodermal derivatives. Furthermore, mutations in EDAR resulted in autosomal dominant and recessive forms of hypohidrotic ectodermal dysplasia.

    • Synonyms

      Ectodysplasin A Receptor, DL, Ectodysplasin 1, Anhidrotic Receptor, Anhidrotic Ectodysplasin Receptor 1, Ectodermal Dysplasia Receptor, Ectodysplasin-A Receptor, Downless Homolog, EDA-A1 Receptor, ECTD10A, ECTD10B, EDA3, HRM1, ED3, Tumor Necrosis Factor Receptor Superfamily Member EDAR, Downless, Mouse, Homolog Of, EDA-A1R, EDA1R, ED1R, ED5, Tumor necrosis factor receptor superfamily member EDAR.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Immunogen

      Anti-human EDAR mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human EDAR protein 27-448 amino acids purified from E. coli.

    • Ig Subclass

      Mouse IgG2a heavy chain and k light chain.

    • Clone

      PAT19E8AT.

    • Applications

      EDAR antibody has been tested by ELISA, Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended starting dilution is 1:1000.

    • Type

      Mouse Anti Human Monoclonal.

    • Storage Procedures

      For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.

    • Purification Method

      EDAR antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.

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

    Edar Antibody
  • View Data Sheet

    Name :

    TXN1 Human, His

    Description:

    Thioredoxin Human Recombinant, His Tag

    Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.

    Product # :

    PRO-804

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    Description

    Thioredoxin Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 125 amino acids (1-105 a.a.) and having a molecular mass of 13.9 kDa (Molecular weight on SDS-PAGE will appear higher). TXN protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    TXN1 solution containing 1x PBS pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is 7-10 A650/min/mg, obtained by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.

    More Info

    • Introduction

      Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation.

    • Synonyms

      Thioredoxin, ATL-derived factor, ADF, Surface-associated sulphydryl protein, SASP, TXN, TRDX, TRX, TRX1, MGC61975, DKFZp686B1993.

    • 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 MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV.

    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.

    Txn1 Human His
  • View Data Sheet

    Name :

    Eptifibatide Human

    Description:

    Eptifibatide Human

    Product # :

    PRO-358

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    Description

    Synthetic Eptifibatide is a 6 amino acid peptide having a MW of 832.5 Dalton the following sequence Mpr-Har-Gly-Asp-Trp-Pro-Cys-NH2.

    Formulation

    Eptifibatide 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

      Eptifibatide binds to the platelet receptor glycoprotein (GP) IIb/IIIa of human platelets and inhibits platelet aggregation. Eptifibatide is a cyclic peptide derived from a protein discovered in the venom of the southeastern pygmy rattlesnake (Sistrurus miliarus barbouri). Eptifibatide belongs to the arginin-glycin-aspartat-mimetics and reversibly binds to platelets.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Eptifibatide
  • View Data Sheet

    Name :

    HTF Human

    Description:

    Holo Transferrin Human

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

    Product # :

    PRO-315

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    Description

    Human Holo Transferrin is a glycoprotein of approximately 77 kDa.

    Source

    Human serum.

    Formulation

    The protein (10mg/ml) was lyophilized from 20mM NH4HC03 solution.
    May contain traces of buffer salts.

    Purity

    Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.

    More Info

    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
      Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered Pink lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Holo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Human Virus Test

      FDA approved Plasma from each donor has been tested and found negative for antibodies to HIV-1 & 2, HCV, HBsAG, HBc, HBV, HAV, HIV and Syphilis.

    • Iron Content

      The Iron content was estimated by ICP and was found to be 1232 ppm.

    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.

    Holo Transferrin Human
  • View Data Sheet

    Name :

    RARRES2 Human, HEK

    Description:

    Retinoic Acid Receptor Responder 2 Human Recombinant, HEK

    Chemerin, TIG2, Tazarotene-induced gene 2 protein, Retinoic acid receptor responder protein 2, RAR-responsive protein TIG2, RARRES2, HP10433.

    Product # :

    PRO-2596

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    Description

    RARRES2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (21-157 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 143 amino acids and having a molecular mass of 16.6kDa. RARRES2 shows multiple bands between 13.5-18kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    HEK293.

    Formulation

    RARRES2 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate buffered saline (pH7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RARRES2 is a secreted chemotactic protein that initiates chemotaxis through the ChemR23 G protein-coupled seven-transmembrane domain ligand. RARRES2 is upregulated by the synthetic retinoid tazarotene and found in many tissues. RARRES2 acts as an adipokine and is truncated on both termini from the proprotein. RARRES2 is structurally related to the cathelicidin precursors, cystatin C and kininogens. RARRES2 promotes calcium mobilization and chemotaxis of immature dendritic cells and macrophages. RARRES2 is secreted as a precursor of little biological activity, which requires proteolytic cleavage of its COOH-terminal domain to be exchangeed into a potent and highly specific agonist of ChemR23.

    • Synonyms

      Chemerin, TIG2, Tazarotene-induced gene 2 protein, Retinoic acid receptor responder protein 2, RAR-responsive protein TIG2, RARRES2, HP10433.

    • 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

      ELTEAQRRGL QVALEEFHKH PPVQWAFQET SVESAVDTPF PAGIFVRLEF KLQQTSCRKR DWKKPECKVR PNGRKRKCLA CIKLGSEDKV LGRLVHCPIE TQVLREAEEH QETQCLRVQR AGEDPHSFYF PGQFAFSHHH HHH.

    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.

    Chemerin Protein
  • View Data Sheet

    Name :

    VEGF (121 a.a.) Human

    Description:

    Vascular Endothelial Growth Factor (121 a.a.) Human Recombinant

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-343

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    Description

    Vascular Endothelial Growth Factor-121 Human Recombinant produced in E.Coli is a non-glycosylated, polypeptide double chain containing 2x121 amino acids and having a molecular mass of 28.4kDa. VEGF121 circulates more freely than other VEGF forms, which bind more tightly with vascular heparin sulfates.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    Biological Activity

    VEGF-121 has full biological activity when compared to standards. The activity is determined by the dose-dependent proliferation of HUVECs and is typically 1-6ng/ml corresponding to a specific activity of 166,667-1,000,000U/mg.

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    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both vasculogenesis and angiogenesis. As its name implies, VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/ macrophagemigration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesisand cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of this protein are linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in this gene have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Vascular Endothelial Growth Factor 121 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VEGF-121 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 Vascular Endothelial Growth Factor -121 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      APMAEGGGQN HHEVVKFMDV YQRSYCHPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCGGC CNDEGLECVP TEESNITMQI MRIKPHQGQH IGEMSFLQHN KCECRPKKDR ARQENCDKPR R

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    Vegf121 Human
  • View Data Sheet

    Name :

    LHRH Human

    Description:

    Luteinizing Hormone Releasing Hormone Human

    Progonadoliberin-1, Progonadoliberin I, LHRH, GRH, GNRH, LNRH.

    Product # :

    HOR-261

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    Description

    Lutenizing Hormone Releasing Hormone Human Synthetic is a single, non-glycosylated, polypeptide chain containing 10 amino acids and having a molecular mass of 1182.2 Dalton. The molecular formula is C55H75N17O13.C2H4O2. The CAS Number is 71447-49-9.

    Formulation

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

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    More Info

    • Introduction

      Gonadotropin-releasing hormone 1 (GNRH1), also known as Luteinising-hormone releasing hormone (LHRH), is a peptide hormone responsible for the release of FSH and LH from the anterior pituitary. GNRH1 is synthesized and released by the hypothalamus.
      At the pituitary, GNRH1 stimulates the synthesis and secretion of the gonadotropins follicle-stimulating hormone (FSH) and luteinizing hormone (LH). These processes are controlled by the size and frequency of GNRH1 pulses, as well as by feedback from androgens and estrogens. Low requency GNRH1 pulses lead to FSH release, whereas high frequency GNRH1 pulses stimulate LH release.
      There are differences in GNRH1 secretion between males and females. In males, GNRH1 is secreted in pulses at a constant frequency, but in females the frequency of the pulses varies during the menstrual cycle and there is a large surge of GNRH1 just before ovulation.
      GNRH1 secretion is pulsatile in all vertebrates, and is necessary for correct reproductive function. Thus, a single hormone, GNRH1, controls a complex process of follicular growth, ovulation, and corpus luteum maintenance in the female, and spermatogenesis in the male.

    • Synonyms

      Progonadoliberin-1, Progonadoliberin I, LHRH, GRH, GNRH, LNRH.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized LHRH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LNRH 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 LHRH in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions. The LHRH is also soluble in a 1% glacial acetic acid.

    • Amino Acid Sequence

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

    Lhrh Human
  • View Data Sheet

    Name :

    Cyclosporin A

    Description:

    Cyclosporin-A

    Product # :

    PRO-408

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Cyclosporin is a cyclic polypeptide immunosuppressant agent consisting of 11 amino acids and having a molecular weight of 1202.64. It is produced as a metabolite by the fungus species Beauveria nlyea. Chemically, cyclosporin is designated as [R-[R*,R*-(E)]]-cyclic(L-alanyl-D- alanyl-N-methyl-L-leucyl-N-methyl-L-leucyl-N-methyl-L-valyl-3-hydroxy-N, 4-dimethyl-L-2-amino-6-octenoyl-L-a-amino-butyryl- N-methylglycyl-N- methyl-L-leucyl-L-valyl-N-methyl-L-leucyl). Molecular Formula: C62H111N11O12.

    Source

    Beauveria Nivea.

    Formulation

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

    Purity

    Greater than 99.0% as determined by RP-HPLC.

    More Info

    • Introduction

      Cyclosporin A is a noncytotoxic, natural, 11 amino acid cyclic peptide used clinically as an immunosuppressant for the treatment of autoimmune and inflammatory disorders and to prevent organ rejection after transplantation. Cyclosporin acts chiefly by inhibiting T lymphocyte function, which is vital for the propagation of inflammation. Cyclosporin A does not suppress the activity of other hematopoietic cells, does not cause bone marrow suppression and has a rapid onset of action as opposed to other immunosuppressive agents. Nevertheless, Cyclosporin A -induced nephrotoxicity remains an important clinical problem, and oxidative stress has been implicated as a potential responsible mechanism.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Cyclosporin A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cyclosporin A 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 Cyclosporin-A in anhydrous ethanol R at a concentration of 50mg/ml.

    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.

    Cyclosporin A
  • View Data Sheet

    Name :

    MT I

    Description:

    Melanotan-I

    Melanotan-I, MT-I, Melanotan-1.

    Product # :

    HOR-306

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

    • description
    • formulation
    • purity
    • More Info

    Description

    Melanotan-I has the amino acid sequence of Ser-Tyr-Ser-Nle-Glu-His-D-Phe-Arg-Trp-Gly-Lys-Pro-Val and a molecular weight of 1647.4 Dalton.

    Formulation

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

    Purity

    Greater than 98.0% as determined by RP-HPLC.

    More Info

    • Synonyms

      Melanotan-I, MT-I, Melanotan-1.

    • Physical Appearance

      Sterile Filtered off-White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Melanotan-I although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MT-I 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 Melanotan-I in sterile 1% acetic acid not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.

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

    Melanotan I
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