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Search results

1000 results found for “Neuropilin”

Name

Description

Product #

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Quantity

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  • View Data Sheet

    Name :

    GABARAPL1 Human

    Description:

    GABA(A) Receptor-Associated Protein Like 1 Human Recombinant

    Gamma-aminobutyric acid receptor-associated protein-like 1, Early estrogen-regulated protein, GABA(A) receptor-associated protein-like 1, Glandular epithelial cell protein 1, GEC-1, GABARAPL1, GEC1, ATG8, APG8L, ATG8B, ATG8L, APG8-LIKE.

    Product # :

    PRO-048

    Price :

    Quantity :

    Shipping Method :

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    Shipped with Ice Packs

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    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    GABARAPL1 Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 137 amino acids (1-117 a.a.) and having a molecular mass of 16.2kDa (Molecular size on SDS-PAGE will appear higher). The GABARAPL1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GABARAPL1 solution (1 mg/ml) contains 20mM Tris buffer (pH 8.0), 10% glycerol, 1mM DTT and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GABARAPL1 [Gamma-aminobutyric acid (GABA) receptor-associated protein-like 1] is a member of the MAP1 LC3 family. GABARAPL1 increases cell surface expression of kappa type opioid receptor through facilitating anterograde intracellular trafficking of the receptor.

    • Synonyms

      Gamma-aminobutyric acid receptor-associated protein-like 1, Early estrogen-regulated protein, GABA(A) receptor-associated protein-like 1, Glandular epithelial cell protein 1, GEC-1, GABARAPL1, GEC1, ATG8, APG8L, ATG8B, ATG8L, APG8-LIKE.

    • 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 MKFQYKEDHP FEYRKKEGEK IRKKYPDRVP VIVEKAPKAR VPDLDKRKYL VPSDLTVGQF YFLIRKRIHL RPEDALFFFV NNTIPPTSAT MGQLYEDNHE EDYFLYVAYS DESVYGK.

    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.

    Gabarapl1 Human
  • View Data Sheet

    Name :

    Vaspin Human

    Description:

    Vaspin Recombinant Human

    Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    Product # :

    CYT-1132

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • description
    • source
    • formulation
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    • Citations

    Description

    Vaspin Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 394 amino acids and having a molecular mass of 45.1kDa. Vaspin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in 20mM Tris-HCl, pH 8.0, 150mM NaCl and 0.02 % Tween-20.

    Purity

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

    Citations

    More Info

    • Introduction

      Vaspin (visceral adipose-specific SERPIN) is a newly identified adipokine, which is a member of serine protease inhibitor family. Vaspin is also a unique insulin sensitizing adipocytokine in obesity. A recent publication indicates that induction of human vaspin mRNA expression in adipose tissue is regulated in a fat depot-specific manner and could be associated with parameters of obesity, insulin resistance, and glucose metabolism.

    • Synonyms

      Serpin A12 precursor, Visceral adipose-specific serpin, Visceral adipose tissue- derived serine protease inhibitor, Vaspin, OL-64, SERPINA12, Serine (or cysteine) proteinase inhibitor, clade A, antitrypsin, alpha-1 antiproteinase.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      LKPSFSPRNY KALSEVQGWK QRMAAKELAR QNMDLGFKLL KKLAFYNPGR NIFLSPLSIS TAFSMLCLGA QDSTLDEIKQ GFNFRKMPEK DLHEGFHYII HELTQKTQDL KLSIGNTLFI DQRLQPQRKF LEDAKNFYSA ETILTNFQNL EMAQKQINDF ISQKTHGKIN NLIENIDPGT VMLLANYIFF RARWKHEFDP NVTKEEDFFL EKNSSVKVPM MFRSGIYQVG YDDKLSCTIL EIPYQKNITA IFILPDEGKL KHLEKGLQVD TFSRWKTLLS RRVVDVSVPR LHMTGTFDLK KTLSYIGVSK IFEEHGDLTK IAPHRSLKVG EAVHKAELKM DERGTEGAAG TGAQTLPMET PLVVKIDKPY LLLIYSEKIP SVLFLGKIVN PIGK.

    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.

    Vaspin Protein
  • View Data Sheet

    Name :

    MANF Human, His

    Description:

    Mesencephalic Astrocyte-Derived Neurotrophic Factor Human Recombinant, His Tag

    Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.

    Product # :

    CYT-133

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    MANF Human Recombinant produced in E. coli is a single polypeptide chain containing 183 amino acids (25-182) and having a molecular mass of 20.8kDa.MANF is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MANF solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.

    • Synonyms

      Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.

    • 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 MGSHMLRPGD CEVCISYLGR FYQDLKDRDV TFSPATIENE LIKFCREARG KENRLCYYIG ATDDAATKII NEVSKPLAHH IPVEKICEKL KKKDSQICEL KYDKQIDLST VDLKKLRVKE LKKILDDWGE TCKGCAEKSD YIRKINELMP KYAPKAASAR TDL

    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.

    Manf Human
  • View Data Sheet

    Name :

    NENF Human

    Description:

    Neudesin Neurotrophic Factor Human Recombinant

    Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.

    Product # :

    CYT-778

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info
    • Citations

    Description

    NENF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 32-172) containing 151 amino acids including a 10 a.a N-terminal His tag and having a molecular mass of 16.9kDa.

    Source

    Escherichia Coli.

    Formulation

    NENF was filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Neudesin Neurotrophic Factor (NENF) is a member of the cytochrome b5 family, MAPR subfamily. NENF contains 1 cytochrome b5 heme-binding domain. NENF exhibits neurotrophic activity and activates phosphorylation of MAPK1/ERK2, MAPK3/ERK1 and AKT1/AKT in primary cultured neurons. NENF doesn’t have mitogenic activity in primary cultured astrocytes. NENF may play a part in neuronal differentiation and may have a transient influence on neural cell proliferation in neural precursor cells. NENF neurotrophic activity is increased by binding to heme. NENF is up-regulated in immortal cells and induced in estrogen receptor positive breast cancer expressing progesterone receptor.

    • Synonyms

      Neudesin, Cell immortalization-related protein 2, Neuron-derived neurotrophic factor, Secreted protein of unknown function, SPUF protein, NENF, CIR2, SPUF, SCIRP10.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

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

    • Amino Acid Sequence

      MKHHHHHHASGQTPRPAERG PPVRLFTEEE LARYGGEEED QPIYLAVKGV VFDVTSGKEF YGRGAPYNAL TGKDSTRGVA KMSLDPADLT HDTTGLTAKE LEALDEVFTK VYKAKYPIVG YTARRILNED GSPNLDFKPE DQPHFDIKDE F.

    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.

    Nenf Human
  • View Data Sheet

    Name :

    Adiponectin Protein

    Description:

    Adiponectin Human Recombinant

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

    Product # :

    CYT-280

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
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    • More Info
    • sds-page
    • Citations

    Description

    The Adiponectin Human recombinant protein is a single, non-glycosilated polypeptide chain produced in E. coli, having a molecular weight of 25.1 kDa and containing 231 amino acids (15-244).

    Source

    Escherichia Coli.

    Formulation

    Acrp30 protein solution contains Phosphate buffered saline pH 7.4 and 1mM DTT.

    Purity

    Acrp30 purity is greater than 90% as determined by SDS-PAGE.

    sds-page

    Adiponectin-sds-page - Product image 1

    Citations

    More Info

    • Introduction

      The adipose tissue exclusively expresses and secretes Adiponectin (Acrp30). Acrp30 is involved in various physiological processes such as energy homeostasis, insulin sensitivity, hormonal processes, fatty acid metabolism and obesity.
      Adiponectin circulates in the plasma. Decreased levels of Adiponectin are associated with insulin resistance and hyperinsulinemia, as seen in people with obesity insulin resistance, and diabetes type 2, whose plasma levels of adiponectin are reduced.
      The modular structure of Acrp30 is comprised of N-terminal collagenous domain followed by a C-terminal globular domain.
      Acrp30 also acts as a significant negative regulator in hematopoiesis and immune systems; it may be involved in ending inflammatory responses through its inhibitory functions. Adiponectin inhibits endothelial NF-kappa-b signaling through a cAMP-dependent pathway, it also inhibits TNF-alpha- induced expression of endothelial adhesion molecules.

    • Synonyms

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

    • 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

      MGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGE
      KGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSV
      GLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKD
      VKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGE
      RNGLYADNDNDSTFTGFLLYHDTN.

    • Background

      Adiponectin Human Recombinant: Unraveling its Potential in Therapeutic Applications

      1. Abstract

      This paper aims to deliver an extensive exploration into Adiponectin Human Recombinant, a vital adipokine implicated in a multitude of metabolic processes. By delving into the structure, biological roles, and signaling pathways of adiponectin, we elucidate its contribution to pathophysiological conditions. Moreover, we examine the potential therapeutic application of adiponectin in metabolic and cardiovascular diseases.

      2. Introduction

      Adiponectin, a protein predominantly secreted by adipose tissue, plays an integral part in regulating metabolic processes such as glucose regulation and fatty acid oxidation. Understanding the intricacies of adiponectin's actions could pave the way for innovative therapeutic interventions in diseases like obesity, diabetes, and cardiovascular disease.

      3. Structure and Signaling of Adiponectin

      Adiponectin is a 30kDa protein consisting of a collagen-like domain and a C-terminal globular domain. It signals through adiponectin receptors AdipoR1 and AdipoR2, which then activate several intracellular signaling pathways, including AMP-activated protein kinase (AMPK) and peroxisome proliferator-activated receptor-alpha (PPAR-α), regulating various metabolic processes.

      4. Biological Functions of Adiponectin

      Adiponectin has been shown to enhance insulin sensitivity, stimulate fatty acid oxidation, and exert anti-inflammatory effects. Additionally, it is involved in regulating energy homeostasis and has been linked to the regulation of food intake and body weight.

      5. Adiponectin in Disease Pathology

      Reduced levels of adiponectin have been associated with obesity, insulin resistance, type 2 diabetes, and cardiovascular disease. Moreover, adiponectin deficiency has been observed in metabolic syndrome, emphasizing the adipokine's crucial role in metabolic health.

      6. Therapeutic Potential of Adiponectin

      Given adiponectin's role in metabolic regulation, its potential as a therapeutic target is of considerable interest. Approaches to increase circulating adiponectin levels or enhance adiponectin signaling could offer potential therapeutic strategies for managing metabolic diseases and cardiovascular conditions.

      7. Conclusion and Future Perspectives

      While our understanding of adiponectin and its role in health and disease has greatly advanced in recent years, there is still much to uncover. Further research on the precise molecular mechanisms of adiponectin could pave the way for novel therapeutic approaches.

      What is the molecular weight / Mw of ADIPONECTIN Protein?
      ADIPONECTIN Protein has a total Mw of 25.1kDa.
      What is the source or expression system of ADIPONECTIN Protein?
      Escherichia Coli.

      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?
      MGHDQETTTQGPGVLLPLPKGACTGWMAGIPGHPGHNGAPGRDGRDGTPGE
      KGEKGDPGLIGPKGDIGETGVPGAEGPRGFPGIQGRKGEPGEGAYVYRSAFSV
      GLETYVTIPNMPIRFTKIFYNQQNHYDGSTGKFHCNIPGLYYFAYHITVYMKD
      VKVSLFKKDKAMLFTYDQYQENNVDQASGSVLLHLEVGDQVWLQVYGEGE
      RNGLYADNDNDSTFTGFLLYHDTN..

      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
  • View Data Sheet

    Name :

    GABARAPL2 Human

    Description:

    GABA(A) Receptor-Associated Protein Like 2 Human Recombinant

    GABA(A) receptor-associated protein-like 2, GATE-16, GEF2, ATG8, ATG8C, Ganglioside expression factor 2, General protein transport factor p16, Golgi-associated ATPase enhancer of 16 kDa, MAP1 light chain 3-related protein, gamma-aminobutyric acid receptor-associated protein-like 2, MAP1 light chain 3 related protein, FLC3A.

    Product # :

    PRO-079

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    Description

    GABARAPL2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 137 amino acids (1-117a.a.) and having a molecular mass of 15.8kDa. GABARAPL2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GABARAPL2 protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GABARAPL2 takes part in intra Golgi traffic and modulates intra Golgi transport by coupling between NSF activity and SNAREs activation. GABARAPL2 first stimulates the ATPase activity of NSF which in turn stimulates the association with GOSR1.

    • Synonyms

      GABA(A) receptor-associated protein-like 2, GATE-16, GEF2, ATG8, ATG8C, Ganglioside expression factor 2, General protein transport factor p16, Golgi-associated ATPase enhancer of 16 kDa, MAP1 light chain 3-related protein, gamma-aminobutyric acid receptor-associated protein-like 2, MAP1 light chain 3 related protein, FLC3A.

    • 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MKWMFKEDHS LEHRCVESAK IRAKYPDRVP VIVEKVSGSQ IVDIDKRKYL VPSDITVAQF MWIIRKRIQL PSEKAIFLFV DKTVPQSSLT MGQLYEKEKD EDGFLYVAYS GENTFGF

    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.

    Gabarapl2 Human
  • View Data Sheet

    Name :

    Noggin Human

    Description:

    Noggin Human Recombinant

    SYM1, SYNS1, NOG.

    Product # :

    CYT-475

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    Description

    Noggin Human Recombinant produced in E.Coli is a non-glycosylated, non-disulfide-linked homodimer consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.3kDa. Noggin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered solution in 30% CH3CN, 0.1% TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was determined by its ability to inhibit 5.0ng/ml of BMP-4 induced alkaline phosphatase production by murine ATDC-5 cells. The expected ED50 for this effect  is < 3ng/ml of Noggin, corresponding to a Specific Activity of 3.3x105units/mg.

    Citations

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    • Introduction

      The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

    • Synonyms

      SYM1, SYNS1, NOG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HCl to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYDPGFMATSPP
      EDRPGGGGGAAGGAEDLAELDQLLRQRPSGAMPSEIKGLEFSEGLAQGKKQRLSKKLR
      RKLQMWLWSQTFCPVLYAWNDLGSRFWPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHL
      TVLRWRCQRRGGQRCGWIPIQYPIISECKCSC.

    • Background

      Recombinant Human Noggin Growth Beta Factor: A Potent Inhibitor of Bone Morphogenetic Protein Signaling.

      Abstract:

      Recombinant human Noggin Growth Beta Factor (Noggin) is a highly conserved protein that acts as a potent antagonist of the Bone Morphogenetic Protein (BMP) signaling pathway.

      Noggin plays a critical role in embryonic development, tissue homeostasis, and disease processes.

      This research paper provides a comprehensive analysis of the molecular characteristics, signaling mechanisms, and diverse physiological functions of recombinant human Noggin.

      Additionally, it explores the therapeutic implications of Noggin in various disorders. Synonyms such as SYM1, SYNS1, and NOG associated with Noggin are discussed throughout the paper to highlight their relevance in scientific literature.

      Introduction:

      1. Recombinant human Noggin Growth Beta Factor (Noggin) is a protein with multifaceted roles in development, tissue homeostasis, and disease. This section introduces Noggin and its synonyms, including SYM1, SYNS1, and NOG, emphasizing their significance and relevance in scientific research.

      Molecular Characteristics of Noggin :

      1. This section explores the molecular characteristics of Noggin, including its primary amino acid sequence, protein structure, and post-translational modifications. The interactions of Noggin with BMPs and other regulatory molecules are also discussed, highlighting the importance of these interactions in modulating BMP signaling.

      Inhibition of BMP Signaling by Noggin:

      1. Noggin acts as a potent inhibitor of BMP signaling by binding to BMP ligands and preventing their interaction with BMP receptors. This section delves into the mechanisms through which Noggin interferes with BMP signaling, including competition for receptor binding and sequestration of BMPs in extracellular spaces. The implications of Noggin-mediated inhibition of BMP signaling in development and tissue homeostasis are also discussed.

      Physiological Functions of Noggin:

      1. Noggin plays critical roles in various physiological processes, including embryonic development, neurogenesis, skeletal development, and joint formation. This section provides an in-depth analysis of Noggin's contributions to these processes, highlighting its role in maintaining proper tissue patterning, cell fate determination, and morphogenesis.

      Therapeutic Implications of Noggin:

      1. The unique inhibitory properties of Noggin make it an attractive therapeutic candidate for various disorders. This section discusses the potential applications of Noggin in bone and joint diseases, neurological disorders, and cancer. Additionally, it explores the challenges and future prospects of utilizing Noggin as a therapeutic agent.

      Clinical Studies and Translational Research:

      1. This section reviews clinical studies and translational research involving Noggin, emphasizing its potential in regenerative medicine and tissue engineering. It highlights ongoing efforts to develop Noggin-based therapeutics and discusses the promising results observed in preclinical and clinical 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.

    Noggin Human
  • View Data Sheet

    Name :

    PSPN Mouse

    Description:

    Persephin Mouse Recombinant

    Persephin, PSPN.

    Product # :

    CYT-802

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    Description

    PSPN Mouse Recombinant produced in E.Coli is a disulfide-linked homodimer containing 2x96 amino acids and having a molecular mass of 20.7kDa. The PSPN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2?m filtered concentrated solution in 30 %ACN, 0.1 %TFA, 150mM NaCl.

    Purity

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

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as determined by a cell proliferation assay using human TT medullary thyroid cancer cells is less than 0.1ng/ml, corresponding to a specific activity of > 1.0 × 10,000,000 IU/mg. 

    Citations

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    • Introduction

      Persephin is a member of the GDNF ligand subfamily of the TGF-beta superfamily. PSPN encourages the existence and growth of key dopaminergic and motor neurons, as well as taking part in kidney development. Nonetheless, persephin does not support existence of peripheral neurons.

    • Synonyms

      Persephin, PSPN.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      ALAGSCRLWS LTLPVAELGL GYASEEKVIF RYCAGSCPQE ARTQHSLVLA RLRGRGRAHG RPCCQPTSYA DVTFLDDQHH WQQLPQLSAA ACGCGG

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    Pspn Mouse
  • View Data Sheet

    Name :

    Pleiotrophin Human

    Description:

    Pleiotrophin Human Recombinant

    PTN, Heparin Affin Regulatory Protein, HARP, Heparin-binding growth factor-8, HBGF-8, Osteoblast-Specific Factor-1, OSF-1, Heparin-binding growth-associated molecule, HB-GAM, HBNF-1 Heparin-binding brain mitogen, Heparin-binding neurite outgrowth-promoting factor 1, HBBM, NEGF1.

    Product # :

    CYT-749

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    Description

    Pleiotrophin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 136 amino acids and having a molecular mass of 15.3kDa.The Pleiotrophin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Pleiotrophin protein was lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

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

    sds-page

    Pleiotrophin Human SDS-PAGE - Product image 1

    Citations

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    • Introduction

      Pleiotrophin (Osteoblast-Specific Factor-1, OSF-1) contains 136 amino acid residues. The sequence is very rich in cationic amino acids (24% of the residues); lysine cluster sequences are found in the N-terminal and C-terminal ends of the structure.
      The OSF-1 gene was shown by Northern blotting analysis to be expressed in mouse calvarial osteoblast-enriched cells and in mouse brain tissues, but not in thymus, spleen, kidney, liver, lung, testis or heart. Pleiotrophin has the ability to promote adhesion, migration, expansion, and differentiation of human osteoprogenitor cells. In addition to certain types of cancer, the embryonic growth and differentiation factor pleiotrophin is found also in adults in inflammatory diseases. In osteoarthritis, pleiotrophin is especially expressed in early stages, and its concentrations in the synovial fluid could serve as a marker for the progress of the disease. Pleitrophin might be involved in cartilage repair in osteoarthritis, in particular, in earlier stages.

    • Synonyms

      PTN, Heparin Affin Regulatory Protein, HARP, Heparin-binding growth factor-8, HBGF-8, Osteoblast-Specific Factor-1, OSF-1, Heparin-binding growth-associated molecule, HB-GAM, HBNF-1 Heparin-binding brain mitogen, Heparin-binding neurite outgrowth-promoting factor 1, HBBM, NEGF1.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      GKKEKPEKKV KKSDCGEWQW SVCVPTSGDC GLGTREGTRT GAECKQTMKT QRCKIPCNWK KQFGAECKYQ FQAWGECDLN TALKTRTGSL KRALHNAECQ KTVTISKPCG KLTKPKPQAE SKKKKKEGKK QEKMLD.

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    Pleiotrophin
  • View Data Sheet

    Name :

    SERPINA3 Human

    Description:

    Alpha-1 AntiChymotrypsin Human

    Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.

    Product # :

    PRO-378

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    Description

    Human Alpha-1 AntiChymotrypsin produced from normal human serum having a molecular mass of 68kDa.

    Source

    Human Serum.

    Formulation

    Lyophilized from 0.02M Tris-buffer,pH-7.5 and 0.15M Nacl.

    Purity

    Greater than 90.0%.

    Citations

    More Info

    • Introduction

      Alpha 1 ACT is an early-stage acute-phase plasma protein and a serpin that preferentially inactivates chymotrypsin, cathepsin G, and chymase. Alpha-1- ACT, a serine protease inhibitor, is tightly associated with amyloid plaques in Alzheimer's disease (AD) and in normal aged human and monkey brain.
      Regulation of the serine proteases and serine protease inhibitors plays an important role in neuromuscular differentiation. Prostate specific antigen (PSA), a chymotrypsin-like serine protease, is predominantly complexed to Alpha-1-ACT.

    • Synonyms

      Alpha-1-antichymotrypsin, ACT, Cell growth-inhibiting gene 24/25 protein, SERPINA3, AACT, A1ACT, GIG24, GIG25, MGC88254.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Human SERPINA3 although stable at room temperature for 3 weeks, should be stored between 2-8°C. Do not freeze.

    • Solubility

      It is recommended to reconstitute the lyophilized human A1ACT in sterile 18MΩ-cm H2O at 1mg/ml, which can then be further diluted to other aqueous solutions.

    • Human Virus Test

      Starting material tested and found negative for HIV I & II antibodies, Hepatitis B surface antigen, and Hepatitis C antibodies.

    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.

    Serpina3 Human
  • View Data Sheet

    Name :

    Adiponectin Human, HEK

    Description:

    Adiponectin Human Recombinant, HEK

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

    Product # :

    CYT-434

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    Description

    Acrp30 Human Recombinant produced in HEK cells is a glycosylated polypeptide chain containing 234 amino acids (19-244a.a.) and having a molecular mass of 25.5kDa. Acrp30 is expressed with a FLAG tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    HEK293 (Human Embryonic Kidney cell line).

    Formulation

    Filtered (0.4µm) and lyophilized from 0.5mg/ml in 50mM phosphate Buffer, 75mM NaCl, pH 7.4.

    Purity

    Greater than 98% as determined by HPLC and SDS PAGE.

    Biological Activity

    In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

    sds-page

    adiponectin human HEK sds-page - Product image 1

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    • 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

      White lyophilized (freeze-dried) powder.

    • Stability

      For long term, store lyophilized AdipoQ 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. The lyophilized protein remains stable for 24 months when stored at -20°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

      ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.

    • Background

      What is the molecular weight/Mw of adiponectin Protein?
      Adiponectin Protein has a total Mw of 25.5kDa.

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

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

      What is the Biological Activity of adiponectin Protein?
      In vitro gluconeogenesis assay in primary hepatocytes was performed, showing the Adiponectin human derived from mammalian cells can inhibit glucose production. The ED50 was ~6 µg/ml.

      What is the amino acid sequence of adiponectin Protein?
      ETTTQGPGVL LPLPKGACTG WMAGIPGHPG HNGAPGRDGR DGTPGEKGEK GDPGLIGPKG DIGETGVPGA EGPRGFPGIQ GRKGEPGEGA YVYRSAFSVG LETYVTIPNM PIRFTKIFYN QQNHYDGSTG KFHCNIPGLY YFAYHIVYMK DVKVSLFKKD KAMLFTYDQY QENNVDQASG SVLLHLEVGD QVWLQVYGEG ERNGLYADND NDSTFTGFLL YHDTNDYKDDDDK.

      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 Hek
  • View Data Sheet

    Name :

    NPL Human

    Description:

    N-acetylneuraminate Pyruvate Lyase Human Recombinant

    N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.

    Product # :

    ENZ-125

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    Description

    NPL produced in E.Coli is a single, non-glycosylated polypeptide chain containing 340 amino acids (1-320 a.a.) and having a molecular mass of 37.3kDa.NPL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      N-acetylneuraminate lyase (NPL) is an enzyme which catalyzes the chemical reaction (N-acetylneuraminate ->N-acetyl-D-mannosamine + pyruvate). NPL is a member of a family of lyases, specifically the oxo-acid-lyases, which cleave carbon-carbon bonds. NPL participates in amino sugars metabolism.

    • Synonyms

      N-acetylneuraminate lyase, NALase, N-acetylneuraminate pyruvate-lyase, N-acetylneuraminic acid aldolase, Sialate lyase, Sialate-pyruvate lyase, Sialic acid aldolase, Sialic acid lyase, NPL, C1orf13, NAL, C112, NPL1.

    • 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 MAFPKKKLQG LVAATITPMT ENGEINFSVI GQYVDYLVKE QGVKNIFVNG TTGEGLSLSV SERRQVAEEW VTKGKDKLDQ VIIHVGALSL KESQELAQHA AEIGADGIAV IAPFFLKPWT KDILINFLKE VAAAAPALPF YYYHIPALTG VKIRAEELLD GILDKIPTFQ GLKFSDTDLL DFGQCVDQNR QQQFAFLFGV DEQLLSALVM GATGAVGSTY NYLGKKTNQM LEAFEQKDFS LALNYQFCIQ RFINFVVKLG FGVSQTKAIM TLVSGIPMGP PRLPLQKASR EFTDSAEAKL KSLDFLSFTD LKDGNLEAGS.

    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.

    Npl Human
  • View Data Sheet

    Name :

    NTS Human

    Description:

    Neurotensin Human Recombinant

    NTS, Neurotensin, NT/N, NMN-125, NTS1, NN, Neurotensin/Neuromedin N, NT.

    Product # :

    PRO-1311

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    Description

    NTS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 172 amino acids (24-170 a.a.) and having a molecular mass of 19.9kDa.NTS is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Neurotensin (NTS) is a common precursor for 2 peptides, neuromedin N and neurotensin. Neurotensin is a secreted tridecapeptide, which is generally distributed throughout the central nervous system, and may serve as a neurotransmitter or a neuromodulator. NTS is involved in the maintenance of gut structure and function, and in the regulation of fat metabolism. Tissue-specific processing may initiate the formation in some tissues of larger forms of neuromedin N and neurotensin. The large forms may embody more stable peptides which are also biologically active.

    • Synonyms

      NTS, Neurotensin, NT/N, NMN-125, NTS1, NN, Neurotensin/Neuromedin N, NT.

    • 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 MGSHMSDSEE EMKALEADFL TNMHTSKISK AHVPSWKMTL LNVCSLVNNL NSPAEETGEV HEEELVARRK LPTALDGFSL EAMLTIYQLH KICHSRAFQH WELIQEDILD TGNDKNGKEE VIKRKIPYIL KRQLYENKPR RPYILKRDSY YY.

    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.

    Nts Human
  • View Data Sheet

    Name :

    bNGF Human, CHO

    Description:

    Beta-Nerve Growth Factor Human Recombinant, CHO

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

    Product # :

    CYT-246

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    Description

    Nerve Growth Factor-beta Human Recombinant produced in CHO 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.The NGF-b is purified by proprietary chromatographic techniques.

    Source

    Chinese Hamster Ovary Cells.

    Formulation

    The protein was lyophilized from a 0.2µm filtered solution in 20mM PB and 250mM NaCl, pH 7.0.

    Purity

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

    Biological Activity

    The ED50, calculated by its ability to stimulate chick E9 DRG neurite outgrowth was found to be < 1.0 ng/ml, corresponding to a specific activity of > 1 x 106 units/mg.

    Citations

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

    • Amino Acid Sequence

      Was analyzed by Mass spectrometry.

    • 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?
      Chinese Hamster Ovary Cells.

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

      What is the Biological Activity of B NGF Protein?
      The ED50, calculated by its ability to stimulate chick E9 DRG neurite outgrowth was found to be < 1.0 ng/ml, corresponding to a specific activity of > 1 x 106 units/mg.

      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.

    Beta Ngf Human Cho
  • View Data Sheet

    Name :

    SERPINA1

    Description:

    Alpha 1 Antitrypsin Human

    Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, SERPINA1, A1AT, PI, A1A, AAT, PI1, MGC9222, PRO2275, MGC23330.

    Product # :

    PRO-456

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    Description

    SERPINA1 extracted from human serum and having a 54kDa molecular weight is purified by proprietary chromatographic techniques.

    Formulation

    SERPINA1 is 0.02M NH4HCO3.



    Purity

    Greater than 96% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SERPINA1 is secreted and is a serine protease inhibitor which its targets include elastase, plasmin, collagenase, thrombin, leucocytic proteases, trypsin, chymotrypsin, and plasminogen activator. Defects in SERPINA1 gene can cause emphysema or liver disease. Antral SERPINA1 expression is particularly induced by H. pylori infection. lung and prostate cancers have shown a significant increase in SERPINA1 serum levels compared with healthy controls though breast cancers did not show a significant change. SERPINA1 is an endogenous inhibitor of serine proteases and inhibits the catalytic domain of human recombinant matriptase in vitro. Rise in SERPINA1 occurs as an acute phase response to tissue necrosis and inflammation. mutations in SERPINA1 and SLC11A1 genes change the balance between elastase produced by leukocytes during phagocytosis.

    • Synonyms

      Alpha-1-antitrypsin, Alpha-1 protease inhibitor, Alpha-1-antiproteinase, SERPINA1, A1AT, PI, A1A, AAT, PI1, MGC9222, PRO2275, MGC23330.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SERPINA1 should be stored at 4°C.

    • Solubility

      It is recommended to reconstitute the lyophilized SERPINA1 in 0.15M NaCl, 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.

    Serpina1 Human
  • View Data Sheet

    Name :

    NEU1 Human

    Description:

    Sialidase 1 Human Recombinant

    Sialidase 1 (lysosomal sialidase), Acetylneuraminyl hydrolase, N-acetyl-alpha-neuraminidase 1, exo-alpha-sialidase, Lysosomal sialidase, G9 sialidase, NEU, NANH, SIAL1, EC 3.2.1.18.

    Product # :

    ENZ-645

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    Description

    NEU1 Human Recombinant produced in E. coli is a single polypeptide chain containing 393 amino acids (48-415) and having a molecular mass of 42.9 kDa.NEU1 is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The NEU1 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Sialidase 1 (NEU1) is a lysosomal enzyme which cleaves terminal sialic acid residues from substrates such as glycoproteins and glycolipids. In the lysosome, the NEU1 enzyme is part of a heterotrimeric complex in cooperation with beta-galactosidase and cathepsin A. NEU1 gene mutations may lead to sialidosis, a lysosomal storage disease that can be the type 1 (cherry red -myoclonus syndrome or normosomatic type), which is late-onset, or the type 2 (the dysmorphic type), which takes place at an earlier age with increased acuteness.

    • Synonyms

      Sialidase 1 (lysosomal sialidase), Acetylneuraminyl hydrolase, N-acetyl-alpha-neuraminidase 1, exo-alpha-sialidase, Lysosomal sialidase, G9 sialidase, NEU, NANH, SIAL1, EC 3.2.1.18.

    • 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 MGSHMENDFG LVQPLVTMEQ LLWVSGRQIG SVDTFRIPLI TATPRGTLLA FAEARKMSSS DEGAKFIALR RSMDQGSTWS PTAFIVNDGD VPDGLNLGAV VSDVETGVVF LFYSLCAHKA GCQVASTMLV WSKDDGVSWS TPRNLSLDIG TEVFAPGPGS GIQKQREPRK GRLIVCGHGT LERDGVFCLL SDDHGASWRY GSGVSGIPYG QPKQENDFNP DECQPYELPD GSVVINARNQ NNYHCHCRIV LRSYDACDTL RPRDVTFDPE LVDPVVAAGA VVTSSGIVFF SNPAHPEFRV NLTLRWSFSN GTSWRKETVQ LWPGPSGYSS LATLEGSMDG EEQAPQLYVL YEKGRNHYTE SISVAKISVY GTL

    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.

    Neu1 Human
  • View Data Sheet

    Name :

    NRIP3 Human

    Description:

    Nuclear Receptor-Interacting Protein 3 Human Recombinant

    C11orf14, NY-SAR-105, Nuclear receptor-interacting protein 3, Sarcoma antigen NY-SAR-105, NRIP3.

    Product # :

    PRO-1384

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    Description

    NRIP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 264 amino acids (1-241 a.a.) and having a molecular mass of 29.4kDa. NRIP3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    NRIP3 protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Nuclear Receptor-Interacting Protein (NRIP3)is a 241 amino acid protein which is encoded by a gene that maps to human chromosome 11.Diseases associated with NRIP3 include sarcoma, and acute myeloid leukemia.

    • Synonyms

      C11orf14, NY-SAR-105, Nuclear receptor-interacting protein 3, Sarcoma antigen NY-SAR-105, NRIP3.

    • 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 MGSMFYSGLL TEGGRKETDM REAASLRQQR RMKQAVQFIH KDSADLLPLD GLKKLGSSKD MQPHNILQRR LMETNLSKLR SGPRVPWASK TNKLNQAKSE GLKKSEEDDM ILVSCQCAGK DVKALVDTGC LYNLISLACV DRLGLKEHVK SHKHEGEKLS LPRHLKVVGQ IEHLVITLGS LRLDCPAAVV DDNEKNLSLG LQTLRSLKCI INLDKHRLIM GKTDKEEIPF VETVSLNEDN TSEA.

    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.

    Nrip3 Human
  • View Data Sheet

    Name :

    NUP62 Human

    Description:

    Nucleopurin 62kDa Human Recombinant

    Nuclear pore glycoprotein p62, 62 kDa nucleoporin, Nucleoporin Nup62, NUP62, p62, IBSN, SNDI.

    Product # :

    PRO-999

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    Description

    NUP62 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 66 kDa. NUP62 is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    NUP62 is supplied in 20mM HEPES buffer pH-8, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Nucleopurin 62kDa (NUP62) belongs to the FG-repeat containing nucleoporins and is localized to the nuclear pore central plug. Nucleoporins are the principal components of the nuclear pore complex in eukaryotic cells. This complex is a colossal structure which extends across the nuclear envelope, forming an entryway that regulates the stream of macromolecules between the nucleus and the cytoplasm. NUP62 associates with the importin alpha/beta complex that is involved in the import of proteins containing nuclear localization signals. Defects in the NUP62 are the cause of SNDI (infantile striatonigral degeneration), aka infantile bilateral striatal necrosis (IBSN) or familial striatal degeneration.

    • Synonyms

      Nuclear pore glycoprotein p62, 62 kDa nucleoporin, Nucleoporin Nup62, NUP62, p62, IBSN, SNDI.

    • 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-type human auto-antibodies.2. Standard ELISA test (checker-board analysis of positive/negative sera), immunodot analysis with positive/negative samples.

    • coating concentration

      0.5-1.0 µg/ml (depending on the type of ELISA plate and coating buffer). Suitable for labeling of functional groups.

    • Applications

      Western blot with Polyclonal anti-Nup62 antibodies.

    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.

    Nup62 Human
  • View Data Sheet

    Name :

    NCS1 213 a.a. Human

    Description:

    Neuronal Calcium Sensor 1 213 a.a. Human Recombinant

    Neuronal Calcium Sensor 1, Frequenin-Like Ubiquitous Protein, Frequenin-Like Protein, Frequenin Homolog, FREQ, FLUP, Frequenin (Drosophila) Homolog, Frequenin Homolog (Drosophila), FREQ, NCS-1, Neuronal calcium sensor 1.

    Product # :

    PRO-2075

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    Description

    NCS1 213 a.a. Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-190 a.a) and having a molecular mass of 24.3kDa. NCS1 213 a.a. is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    NCS1 213 a.a. protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      NCS1 is part of the neuronal calcium sensor gene family, which encode calcium-binding proteins expressed primarily in neurons. NCS1 regulates G protein-coupled receptor phosphorylation in a calcium-dependent manner and can substitute for calmodulin. NCS1 is related with secretory granules and modulates synaptic transmission and synaptic plasticity. NCS1 regulates GRK1 and substitutes for calmodulin. NCS1 stimulates PI4KB kinase activity and participates in long-term synaptic plasticity through its interaction with PICK1. NCS1 takes part in neuron differentiation through inhibition of the activity of N-type voltage-gated calcium channel.

    • Synonyms

      Neuronal Calcium Sensor 1, Frequenin-Like Ubiquitous Protein, Frequenin-Like Protein, Frequenin Homolog, FREQ, FLUP, Frequenin (Drosophila) Homolog, Frequenin Homolog (Drosophila), FREQ, NCS-1, Neuronal calcium sensor 1.

    • Physical Appearance

      Sterile Filtered clear 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 MGSMGKSNSK LKPEVVEELT RKTYFTEKEV QQWYKGFIKD CPSGQLDAAG FQKIYKQFFP FGDPTKFATF VFNVFDENKD GRIEFSEFIQ ALSVTSRGTL DEKLRWAFKL YDLDNDGYIT RNEMLDIVDA IYQMVGNTVE LPEEENTPEK RVDRIFAMMD KNADGKLTLQ EFQEGSKADP SIVQALSLYD GLV.

    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.

    Ncs1 213 Aa Human
  • View Data Sheet

    Name :

    Noggin Mouse

    Description:

    Noggin Mouse Recombinant

    Noggin, SYM1, SYNS1, NOG.

    Product # :

    CYT-600

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    Description

    Noggin Mouse Recombinant produced in E.Coli is a non-glycosylated, disulfide-linked protein consisting of two 206 amino acid polypeptide chains, having a total molecular mass of approximately 46.4 kDa (each chain 23.2 kDa).

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2μm filtered solution in 30% acetonitrile, 0.1% TFA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 as determined by inhibiting BMP-4-induced alkaline phosphatase production of murine ATDC5 cells is less than 2ng/ml, corresponding to a specific activity of > 5.0 × 105 IU/mg in the presence of 5ng/ml BMP-4.

    Citations

    More Info

    • Introduction

      The secreted polypeptide noggin, encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may have a principal role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. It was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. Recently, several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1) were identified; both SYM1 and SYNS1 have multiple joint fusion as their principal feature, and map to the same region (17q22) as NOG. All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

    • Synonyms

      Noggin, SYM1, SYNS1, NOG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Mouse Noggin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Mouse Noggin 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 be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in 10mM HAc to a concentration of 0.1-1.0 mg/ml. Further dilutions should be made in appropriate buffered solutions.

    • Amino Acid Sequence

      MQHYLHIRPAPSDNLPLVDLIEHPDPIFDPKEKDLNETLLRSLLGGHYD
      PGFMATSPPEDRPGGGGGPAGGAEDLAELDQLLRQRPSGAMPSEIKG
      LEFSEGLAQGKKQRLSKKLRRKLQMWLWSQTFCPVLYAWNDLGSRF
      WPRYVKVGSCFSKRSCSVPEGMVCKPSKSVHLTVLRWRCQRRGQR
      CGWIPIQYPIISECKCSC.

    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.

    Noggin Mouse
  • View Data Sheet

    Name :

    CX3CL1 Rat

    Description:

    Fractalkine Rat Recombinant (CX3CL1)

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

    Product # :

    CHM-005

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    Description

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

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

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

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized FractalkineRat although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Fractalkine should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      QHLGMTKCNI TCHKMTSPIP VTLLIHYQLN QESCGKRAII LETRQHRHFC ADPKEKWVQD AMKHLDHQTA ALTRNG

    • Background

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

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

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

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

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

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

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

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

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

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

    Fractalkine Rat
  • View Data Sheet

    Name :

    GNLY Human

    Description:

    Granulysin Human Recombinant

    LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.

    Product # :

    PRO-852

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    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    • source
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    • Citations

    Description

    GNLY Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 159 amino acids and fused to a double His Tag (N+C terminus) and having a total molecular mass of 18.1 kDa.The GNLY is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GNLY is part of the SAPLIP family and is located in the cytotoxic granules of T cells, which are discharged upon antigen stimulation. GNLY is localized in cytotoxic granules of cytotoxic T lymphocytes and natural killer cells, and it has antimicrobial activity against M. tuberculosis and other organisms. GNLY is an antimicrobial protein that kills intracellular pathogens. GNLY is active against a wide range of microbes, including Gram-positive and Gram-negative bacteria, fungi, and parasites. Kills Mycobacterium tuberculosis.

    • Synonyms

      LAG2, Lymphokine LAG-2, TLA519, NKG5, LAG2, D2S69E, Granulysin, T-cell activation protein 519, GNLY, D2S69E.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHHSSGLVPRGSHMMEGLVFSRLSPEYYD
      LARAHLRDEEKSCPCLAQEGPQGDLLTKTQELGRDYR
      TCLTIVQKLKKMVDKPTQRSVSNAATRVCRTGRSRWR
      DVCRNFMRRYQSRVTQGLVAGETAQQICEDLRLCIPS
      TGPLGSHHHHHH.

    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.

    Gnly Human
  • View Data Sheet

    Name :

    NT 3 Human

    Description:

    Neurotrophin-3 Human Recombinant

    Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.

    Product # :

    CYT-257

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    Description

    Neurotrophin-3 Human Recombinant produced in E.Coli is a non-glycosylated and non-covalently linked homodimer, containing 2x120 amino acid chains, having a total Mw of 27.5 kDa. The NT-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from 0.1% TFA.

    Purity

    Greater than 95.0% as determined by analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by the dose-dependent proliferation of neuroblastoma cell line expressing BR6 is 3.49 ng/ml.

    Citations

    More Info

    • Introduction

      NT3 a member of the neurotrophin family, that controls survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. It may be involved in the maintenance of the adult nervous system, and may affect development of neurons in the embryo when it is expressed in human placenta. NTF3-deficient mice generated by gene targeting display severe movement defects of the limbs. The mature peptide of this protein is identical in all mammals examined including human, pig, rat and mouse.

    • Synonyms

      Neurotrophic factor, Nerve growth factor-2, NGF-2, HDNF, NT-3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized NGF2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution NGF-2 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 Neurotrophin-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MYAEHKSHRGE YSVCDSESLW VTDKSSAIDI RGHQVTVLGE IKTGNSPVKQ YFYETRCKEA RPVKNGCRGI DDKHWNSQCK TSQTYVRALT SENNKLVGWR WIRIDTSCVC ALSRKIGRT.

    • Protein content

      Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 2.165 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of NT-3 as a Reference Standard.

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

    Neurotrophin 3 Human
  • View Data Sheet

    Name :

    Cyclophilin A Mouse

    Description:

    Cyclophilin A Mouse Recombinant

    Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.

    Product # :

    ENZ-857

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    Description

    Cyclophilin A Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-164a.a.) and having a molecular mass of 20.4kDa.Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    Cyclophilin A protein solution (0.5mg/ml) containing Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. Cyclophilin-A is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. Cyclophilin-A can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported.

    • Synonyms

      Peptidyl-prolyl cis-trans isomerase A, PPIase A, Cyclophilin A, Cyclosporin A-binding protein, Rotamase A, SP18, Peptidyl-prolyl cis-trans isomerase A, N-terminally processed, Ppia, 2700098C05 Cphn, CyP-18, CypA.

    • 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 MGSMVNPTVF FDITADDEPL GRVSFELFAD KVPKTAENFR ALSTGEKGFG YKGSSFHRII PGFMCQGGDF TRHNGTGGRS IYGEKFEDEN FILKHTGPGI LSMANAGPNT NGSQFFICTA KTEWLDGKHV VFGKVKEGMN IVEAMERFGS RNGKTSKKIT ISDCGQL.

    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.

    Cyclophilin A Mouse
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