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Search results

505 results found for “density lipoprotein”

Name

Description

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  • View Data Sheet

    Name :

    MIF Rat

    Description:

    Macrophage Migration Inhibitory Factor Rat Recombinant

    Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

    Product # :

    CYT-193

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    • source
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    Description

    MIF Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 115 amino acids and having a molecular mass of 12.5kDa. The MIF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

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

    More Info

    • Introduction

      The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.

    • Synonyms

      Macrophage migration inhibitory factor, MIF, Glutathione-binding 13 kDa protein, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MPMFIVNTNV PRASVPEGFL SELTQQLAQA TGKPAQYIAV HVVPDQLMTF SGTSDPCALC SLHSIGKIGG AQNRNYSKLL CGLLSDRLHI SPDRVYINYY DMNAANVGWN GSTFA.

    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.

    Mif Rat
  • View Data Sheet

    Name :

    CCL18 Human

    Description:

    Macrophage Inflammatory Protein-4 Human Recombinant (CCL18)

    Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.

    Product # :

    CHM-322

    Price :

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    • description
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    • More Info

    Description

    Macrophage Inflammatory Protein-4 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 69 amino acids and having a molecular mass of 7813 Dalton. The MIP-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MIP-4 protein is lyophilized from a 0.2µm filtered concentrated (1.0mg/ml) solution in 20mM PB, pH 7.4, 100mM NaCl.

    Purity

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

    Biological Activity

    The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

    More Info

    • Introduction

      Chemokine (C-C motif) ligand 18 (CCL18 / MIP-4) is a small cytokine belonging to the CC chemokine family that was previously called PARC (pulmonary and activation-regulated chemokine). MIP-4 is approximately 60% identical in amino acid sequence to CCL3. MIP-4 is expressed at high levels in lung and at lower levels in certain lymphoid tissues, such as the lymph nodes, and is chemotactic for activated T cells and non activated lymphocytes. The gene for human CCL18 contains three exons and is located on chromosome 17.

    • Synonyms

      Small inducible cytokine A18, CCL18, Macrophage inflammatory protein 4, MIP-4, Pulmonary and activation-regulated chemokine, CC chemokine PARC, Alternative macrophage activation-associated CC chemokine 1, AMAC-1, Dendritic cell chemokine 1, DC-CK1, chemokine (C-C motif) ligand 18, CKb7, PARC, AMAC1, DCCK1, SCYA18.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized MIP-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution MIP-4 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 MIP-4 in sterile 18M-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 of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.

    • Background

      What is the molecular weight/Mw of CCL18 HUMAN Protein?
      CCL18 HUMAN Protein has a total Mw of 7.8kDa.

      What is the source or expression system of CCL18 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of CCL18 HUMAN Protein?
      CCL18 HUMAN Protein is > 97% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL18 HUMAN Protein?
      The Activity MIP-4 is calculated by the ability to chemoattract Human T lymphocytes at 1-10ng/ml corresponding to a Specific Activity of 100,000-1,000,000IU/mg.

      What is the amino acid sequence of CCL18 HUMAN Protein?
      The sequence of the first five N-terminal amino acids of MIP-4 was determined and found to be Ala-Gln-Val-Gly-Thr.

      What applications can CCL18 HUMAN Protein be used in?
      CCL18 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL18 HUMAN Protein?
      The endotoxin level is minimal, CCL18 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.

    Mip 4 Human
  • View Data Sheet

    Name :

    IGF1 Gilthead Seabream

    Description:

    IGF1 Gilthead Seabream Recombinant

    Somatomedin C, IGF-I, IGFI.

    Product # :

    CYT-295

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • biological activity
    • More Info

    Description

    IGF1 Gilthead SeabreamRecombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 68 amino acids and having a molecular mass of 7545.4 Dalton, the predicted pI=7.72.IGF-1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02% NaHCO3.

    Purity

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

    Biological Activity

    Binding assays of the 125I-Gealthead Seabream IGF1 to Gilthead Seabream or carp (Cyprinus carpio) sera resulted in high specific binding, indicating the existence of one or more IGF-binding proteins. In binding experiments to crude Gilthead Seabream brain homogenate, using human (h) IGF-I as a ligand, the respective IC50 value of hIGF1 was about fourfold lower than that of Gilthead Seabream IGF-1. Recombinant Gilthead Seabream IGF-1 exhibited mitogenic activity in a mouse mammary gland-derived MME-L1 cell line which was approximately 200-fold lower than that of hIGF1. Binding experiments to intact MME-L1 cells suggests that this difference most likely results from a correspondingly lower affinity for IGF1 receptor in these cells. In contrast, the activities of Gilthead Seabream IGF-I and hIGF-I measured by 35S uptake by gill arches from the goldfish (Carassius auratus) were identical, indicating that the recombinant Gilthead Seabream IGF-I is biologically active.

    More Info

    • Introduction

      The somatomedins, or IGFs, comprise a family of peptides that play important roles in mammalian growth and development. IGF1 mediates many of the growth-promoting effects of GH. Early studies showed that GH did not directly stimulate the incorporation of sulfate into cartilage, but rather acted through a serum factor, termed 'sulfation factor,' which later became known as somatomedin. Three main somatomedins have been characterized: somatomedin C (IGF1), somatomedin A (IGF2), and somatomedin B.

    • Synonyms

      Somatomedin C, IGF-I, IGFI.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IGF1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IGF1 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 IGF-1 in sterile 0.4% NaHCO3 adjusted to ph 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSPETLCGAELVDTLQFVCGERGFYFSKPGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSK

    • Background

      What is the molecular weight/Mw of IGF1 GILTHEAD SEABREAM Protein?
      IGF1 GILTHEAD SEABREAM Protein has a total Mw of 7.54kDa.

      What is the source or expression system of IGF1 GILTHEAD SEABREAM Protein?
      Escherichia Coli.

      What is the Purity of IGF1 GILTHEAD SEABREAM Protein?
      IGF1 GILTHEAD SEABREAM Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of IGF1 GILTHEAD SEABREAM Protein?
      Binding assays of the 125I-Gealthead Seabream IGF1 to Gilthead Seabream or carp (Cyprinus carpio) sera resulted in high specific binding, indicating the existence of one or more IGF-binding proteins. In binding experiments to crude Gilthead Seabream brain homogenate, using human (h) IGF-I as a ligand, the respective IC50 value of hIGF1 was about fourfold lower than that of Gilthead Seabream IGF-1. Recombinant Gilthead Seabream IGF-1 exhibited mitogenic activity in a mouse mammary gland-derived MME-L1 cell line which was approximately 200-fold lower than that of hIGF1. Binding experiments to intact MME-L1 cells suggests that this difference most likely results from a correspondingly lower affinity for IGF1 receptor in these cells. In contrast, the activities of Gilthead Seabream IGF-I and hIGF-I measured by 35S uptake by gill arches from the goldfish (Carassius auratus) were identical, indicating that the recombinant Gilthead Seabream IGF-I is biologically active.

      What is the amino acid sequence of IGF1 GILTHEAD SEABREAM Protein?
      MSPETLCGAELVDTLQFVCGERGFYFSKPGYGPNARRSRGIVDECCFQSCELRRLEMYCAPAKTSK

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

      What is the endotoxin level for IGF1 GILTHEAD SEABREAM Protein?
      The endotoxin level is minimal, IGF1 GILTHEAD SEABREAM Protein was purified using conventional chromatography techniques.


    • Protein content

      Somatomedin C quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.60 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a calibrated solution of IGF1 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.

    Igf 1 Denis
  • View Data Sheet

    Name :

    Dengue-2 C-terminal

    Description:

    Dengue-2 Envelope Hydrophobic Domain Recombinant

    Product # :

    DEN-039

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    Description

    The Recombinant Dengue 2 Envelope Hydrophobic Domain e.coli derived contains 225 amino acids (228-485) from dengue 2 envelope. The protein is fused to a His tag at C-terminal and purified by standard chromatography techniques.

    Source

    E.coli.

    Formulation

    PBS.

    Purity

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

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    • Introduction

      Caused by one of four closely related virus serotypes of the genus Flavivirus, family Flaviviridae, each serotype is sufficiently different that there is no cross-protection and epidemics caused by multiple serotypes (hyperendemicity) can occur. In cell culture experiments and mice Morpholino antisense oligos have shown specific activity against Dengue virus.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Dengue 2 Envelope Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Applications

      Immunoassay.

    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.

    Dengue 2 C Terminal
  • View Data Sheet

    Name :

    AMTN Human

    Description:

    Amelotin Human Recombinant

    UNQ689, Amelotin, PRO1329.

    Product # :

    PRO-1301

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    Description

    AMTN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (17-209 a.a.) and having a molecular mass of 22.2kDa.AMTN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    AMTN protein solution (0.5mg/ml) contains mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 20% glycerol and 2mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AMTN is a member of the amelotin family. AMTN is a lately discovered secreted enamel protein. AMTN mainly expressed during the maturation stage of enamel formation. AMTN gathers in a basal lamina-like structure at the interface between ameloblasts and enamel mineral and it co-localizes with one more lately described enamel protein, odontogenic ameloblast- related protein (ODAM(.

    • Synonyms

      UNQ689, Amelotin, PRO1329.

    • 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 MGSLPQLKPA LGLPPTKLAP DQGTLPNQQQ SNQVFPSLSL IPLTQMLTLG PDLHLLNPAA GMTPGTQTHP LTLGGLNVQQ QLHPHVLPIF VTQLGAQGTI LSSEELPQIF TSLIIHSLFP GGILPTSQAG ANPDVQDGSL PAGGAGVNPA TQGTPAGRLP TPSGTDDDFA VTTPAGIQRS THAIEEATTE SANGIQ.

    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.

    Amtn Human
  • View Data Sheet

    Name :

    SPOP Human

    Description:

    Speckle-Type POZ Protein Human Recombinant

    Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.

    Product # :

    PRO-195

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    Description

    SPOP 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 394 amino acids (1-374 a.a.) and having a molecular mass of 44.3kDa. The SPOP is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SPOP solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 5mM DTT, 50% glycerol, 0.2M NaCl and 2mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Speckle-type POZ protein (SPOP) belongs to the Tdpoz family containing one N-terminal MATH (Meprin and TRAF homology) domain and one C-terminal BTB/POZ domain. SPOP inhibits IPF1/PDX1 transactivation of established target promoters, may be by recruiting a repressor complex. SPOP is involved in ubiquitinylation and protein degradation as a result of an interaction with CUL-3.

    • Synonyms

      Speckle-type POZ protein, HIB homolog 1, Roadkill homolog 1, SPOP, TEF2.

    • Physical Appearance

      SPOP is supplied as a 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 MSRVPSPPPP AEMSSGPVAE SWCYTQIKVV KFSYMWTINN FSFCREEMGE VIKSSTFSSG ANDKLKWCLR VNPKGLDEES KDYLSLYLLL VSCPKSEVRA KFKFSILNAK GEETKAMESQ RAYRFVQGKD WGFKKFIRRD FLLDEANGLL PDDKLTLFCE
      VSVVQDSVNI SGQNTMNMVK VPECRLADEL GGLWENSRFT DCCLCVAGQE FQAHKAILAA RSPVFSAMFE HEMEESKKNR VEINDVEPEV FKEMMCFIYT GKAPNLDKMA DDLLAAADKY ALERLKVMCE DALCSNLSVE NAAEILILAD LHSADQLKTQ AVDFINYHAS DVLETSGWKS MVVSHPHLVA EAYRSLASAQ CPFLGPPRKR LKQS.

    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.

    Spop Human
  • View Data Sheet

    Name :

    OSM Human, 209 a.a

    Description:

    Oncostatin M Human Recombinant (209 a.a.)

    OSM, MGC20461, Oncostatin M.

    Product # :

    CYT-639

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    Description

    Oncostatin-M (209 a.a.) Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 209 amino acids and having a molecular mass of 23.9kDa. The Oncostatin-M (209 a.a.) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Oncostatin-M (209 a.a.) was lyophilized from a concentrated (1mg/ml) solution containing 1x PBS pH-7.4.

    Purity

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

    Biological Activity

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

    More Info

    • Introduction

      Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.

    • Synonyms

      OSM, MGC20461, Oncostatin M.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Oncostatin-M (209 a.a.) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin-M (209 a.a.) should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Oncostatin-M (209 a.a.) in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      AAIGSCSKEYRVLLGQLQKQTDLMQDTSRLLDPYIRIQGLDVPKLREHCRERPG
      AFPSEETLRGLGRRGFLQTLNATLGCVLHRLADLEQRLPKAQDLERSGLNIEDL
      EKLQMARPNILGLRNNIYCMAQLLDNSDTAEPTKAGRGASQPPTPTPASDAFQ
      RKLEGCRFLHGYHRFMHSVGRVFKWGESPNRSRRHSPHQALRKGVRR.

    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.

    Oncostatin M Human 209 Aa
  • View Data Sheet

    Name :

    TMOD3 Human

    Description:

    Tropomodulin 3 Human Recombinant

    Tropomodulin-3, Ubiquitous tropomodulin, U-Tmod, TMOD3, UTMOD.

    Product # :

    PRO-1165

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    Description

    TMOD3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 376 amino acids (1-352 a.a) and having a molecular mass of 42kDa.TMOD3 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TMOD3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tropomodulin 3 (TMOD3) is a member of the tropomodulin family. TMOD3 prevents the elongation and depolymerization of the actin filaments at the pointed end. Actin cytoskeleton regulation by filament capping proteins is essential to many dynamic cellular functions. TMOD3 functions as a negative regulator of cell migration; nevertheless the processes behind its cellular functions are unknown. The Tmod/TM complex influences the formation of the short actin protofilament, which sequentially outlines the geometry of the membrane skeleton.

    • Synonyms

      Tropomodulin-3, Ubiquitous tropomodulin, U-Tmod, TMOD3, UTMOD.

    • 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 MGSHMALPFR KDLEKYKDLD EDELLGNLSE TELKQLETVL DDLDPENALL PAGFRQKNQT SKSTTGPFDR EHLLSYLEKE ALEHKDREDY VPYTGEKKGK IFIPKQKPVQ TFTEEKVSLD PELEEALTSA SDTELCDLAA ILGMHNLITN TKFCNIMGSS NGVDQEHFSN VVKGEKILPV FDEPPNPTNV EESLKRTKEN DAHLVEVNLN NIKNIPIPTL KDFAKALETN THVKCFSLAA TRSNDPVATA FAEMLKVNKT LKSLNVESNF ITGVGILALI DALRDNETLA ELKIDNQRQQ LGTAVELEMA KMLEENTNIL KFGYQFTQQG PRTRAANAIT KNNDLVRKRR VEGDHQ.

    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.

    Tmod3 Human
  • View Data Sheet

    Name :

    TNFAIP8 Human

    Description:

    Tumor Necrosis Factor, Alpha-Induced Protein 8 Human Recombinant

    GG2-1; MDC-3.13, SCC-S2, SCCS2, Tumor necrosis factor alpha-induced protein 8, TNF alpha-induced protein 8, Head and neck tumor and metastasis-related protein, NF-kappa-B-inducible DED-containing protein, NDED, TNF-induced protein GG2-1, TNFAIP8.

    Product # :

    CYT-759

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    Description

    TNFAIP8 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 221 amino acids (1-198a.a.) and having a molecular mass of 25kDa. TNFAIP8 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    TNFAIP8 protein solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      TNFAIP8 which is a part of the TNFAIP8 family acts as a negative mediator of apoptosis and takes part in tumor progression. TNFAIP8 suppresses the TNF-mediated apoptosis by inhibiting caspase-8 activity but not the processing of procaspase-8, resulting in inhibition of BID cleavage and activation of caspase-3.

    • Synonyms

      GG2-1; MDC-3.13, SCC-S2, SCCS2, Tumor necrosis factor alpha-induced protein 8, TNF alpha-induced protein 8, Head and neck tumor and metastasis-related protein, NF-kappa-B-inducible DED-containing protein, NDED, TNF-induced protein GG2-1, TNFAIP8.

    • 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 MGSMHSEAEE SKEVATDVFN SKNLAVQAQK KILGKMVSKS IATTLIDDTS SEVLDELYRV TREYTQNKKE AEKIIKNLIK TVIKLAILYR NNQFNQDELA LMEKFKKKVH QLAMTVVSFH QVDYTFDRNV LSRLLNECRE MLHQIIQRHL TAKSHGRVNN VFDHFSDCEF LAALYNPFGN FKPHLQKLCD GINKMLDEEN I.

    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.

    Tnfaip8 Human
  • View Data Sheet

    Name :

    LIN28 Human

    Description:

    LIN28 Human Recombinant

    CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

    Product # :

    PRO-743

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    Description

    Recombinant Human LIN28 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 191 amino acids (42-209) and having a molecular mass of 21.1 kDa.LIN28 is expressed with a 23 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The LIN28 protein solution (0.5mg/ml) contains 20mM Tris-HCl, pH-8, 10% glycerol, 0.1mM PMSF and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE

    More Info

    • Introduction

      LIN28 plays an important role as a 'translational enhancer', leading specific mRNAs to polysomes and therefore increasing the competence of protein synthesis. LIN28 is a marker of undifferentiated human embryonic stem cells and it enhances the efficiency of the formation of induced pluripotent stem (iPS) cells from human fibroblasts. LIN28 binds to the let-7 pre-miRNA and blocks production of the mature let-7 microRNA in mouse embryonic stem cells. Overexpression of LIN28 is associated with human germ-cell tumors.

    • Synonyms

      CSDD1, FLJ12457, LIN-28, LIN28A, Protein lin-28 homolog A, ZCCHC1, Zinc finger CCHC domain-containing protein 1, Lin-28A, LIN28.

    • 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 SSGLVPRGSHRSMGICKWFN VRMGFGFLSM TARAGVALDP PVDVFVHQSK LHMEGFRSLK EGEAVEFTFK KSAKGLESIR VTGPGGVFCI GSERRPKGKS MQKRRSKGDR CYNCGGLDHH AKECKLPPQP KKCHFCQSIS HMVASCPLKA QQGPSAQGKP TYFREEEEEI HSPTLLPEAQ N.

    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.

    Lin28 Human
  • View Data Sheet

    Name :

    Ipamorelin

    Description:

    Ipamorelin

    Ipamorelin

    Product # :

    HOR-024

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    Description

    Ipamorelin Synthetic is a single, non-glycosylated polypeptide chain containing 4 amino acids, having a molecular mass of 711.85 Dalton and a Molecular formula of C38H49N9O5.

    Formulation

    The protein was lyophilized with no additives.

    Purity

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

    More Info

    • Introduction

      Ipamorelin is a peptide selective agonist of the ghrelin/growth hormone secretagogue receptor and a growth hormone secretagogue. Ipamorelin is a pentapeptide that was derived from GHRP1. Ipamorelin significantly increases plasma growth hormone levels in both animals and humans. Like pralmorelin and GHRP-6, ipamorelin does not affect prolactin, FSH, LH or TSH levels. However, unlike GHRP2 and GHRP6, but as growth hormone-releasing hormone (GHRH), ipamorelin does not stimulate the secretion of adrenocorticotropic hormone (ACTH) or cortisol, and is highly selective for inducing the secretion only of GH.

    • Synonyms

      Ipamorelin

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Aib-His-D-2-Nal-D-Phe-Lys-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.

    Ipamorelin
  • View Data Sheet

    Name :

    HFE Human

    Description:

    Hemochromatosis Human Recombinant

    Hereditary hemochromatosis protein, HLA-H, HFE, HLAH, HH, HFE1, MVCD7, TFQTL2.

    Product # :

    PRO-1332

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    Description

    HFE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 308 amino acids (23-306 a.a) and having a molecular mass of 35.7kDa.HFE is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Hemochromatosis (HFE) is a member of the MHC class I family. The Hemochromatosis protein contains 1 Ig-like C1-type (immunoglobulin-like) domain. HFE is a membrane protein, which is similar to MHC class I-type proteins and associates with beta-2 microglobulin (beta2M). It is assumed that the HFE protein acts to regulate iron absorption by regulating the interaction of the transferrin receptor (TFR) with transferrin. HFE binds to transferrin receptor (TFR) and reduces its affinity for iron-loaded transferrin.

    • Synonyms

      Hereditary hemochromatosis protein, HLA-H, HFE, HLAH, HH, HFE1, MVCD7, TFQTL2.

    • 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 MGSMRLLRSH SLHYLFMGAS EQDLGLSLFE ALGYVDDQLF VFYDHESRRV EPRTPWVSSR ISSQMWLQLS QSLKGWDHMF TVDFWTIMEN HNHSKESHTL QVILGCEMQE DNSTEGYWKY GYDGQDHLEF CPDTLDWRAA EPRAWPTKLE WERHKIRARQ NRAYLERDCP AQLQQLLELG RGVLDQQVPP LVKVTHHVTS SVTTLRCRAL NYYPQNITMK WLKDKQPMDA KEFEPKDVLP NGDGTYQGWI TLAVPPGEEQ RYTCQVEHPG LDQPLIVIWE PSPSGTLV.

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    Hfe Human
  • View Data Sheet

    Name :

    ARF4 Human

    Description:

    ADP-Ribosylation Factor 4 Human Recombinant

    ADP-ribosylation factor 4, ARF4, ARF2.

    Product # :

    PRO-066

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    Description

    ARF4 Human Recombinant fused with a 24 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 204 amino acids (1-180 a.a.) and having a molecular mass of 23kDa. The ARF4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ARF4 solution (0.5 mg/ml) in 20mM Tris-HCl buffer (pH8.0), 0.2M NaCl, 5mM DTT and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ARF4 belongs to the ARF gene family whose members encode small guanine nucleotide-binding proteins which stimulate the ADP-ribosyltransferase activity of cholera toxin and have a role in vesicular trafficking and as activators of phospholipase D. The ARF proteins include five ARF proteins and eleven ARF-like proteins and constitute one family of the RAS superfamily. They are classified as class I, class II and class III; the ARF4 gene is a class II member. The members of each class share a common gene organization. The ARF4 gene spans approximately 12kb and contains 6 exons and 5 introns. The ARF4 gene is the most divergent member of the human ARFs.

    • Synonyms

      ADP-ribosylation factor 4, ARF4, ARF2.

    • 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 MGSHMGLTIS SLFSRLFGKK QMRILMVGLD AAGKTTILYK LKLGEIVTTI PTIGFNVETV EYKNICFTVW DVGGQDRIRP LWKHYFQNTQ GLIFVVDSND RERIQEVADE LQKMLLVDEL RDAVLLLFAN KQDLPNAMAI SEMTDKLGLQ SLRNRTWYVQ ATCATQGTGL YEGLDWLSNE LSKR.

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    Arf4 Human
  • View Data Sheet

    Name :

    BD 4 Rat

    Description:

    BD 4 Rat

    Beta-defensin 4, BD-4, BD-2, Defensin, beta 4, RBD-2, RBD-4, Defb4, Defb2, Defb3.

    Product # :

    CYT-066

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    Description

    BD-4 Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.4kDa.The BD-4 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BD-4 protein was 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

    Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 5-50µg/ml.

    More Info

    • Introduction

      Defensins are cationic peptides with a large spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The Alpha defensins are differentiated from the Beta-defensins by the pairing of their 3 disulfide bonds.
      4 human Beta-defensins have been identified to date; BD-1, BD-2, BD-3 and BD-4.
      Beta-defensins are expressed on some leukocytes and at epithelial surfaces.
      In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The beta-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. Beta-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. Beta-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.

    • Synonyms

      Beta-defensin 4, BD-4, BD-2, Defensin, beta 4, RBD-2, RBD-4, Defb4, Defb2, Defb3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QSINNPITCL TKGGVCWGPC TGGFRQIGTC GLPRVRCCKK K.

    • Background

      What is the molecular weight/Mw of BD4 Protein?
      BD4 Protein has a total Mw of 4.4kDa.

      What is the source or expression system of BD4 Protein?
      Escherichia Coli.

      What is the Purity of BD4 Protein?
      BD4 Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BD4 Protein?
      Measured by its antimicrobial activity against E. coli. The ED50 for this effect is typically 5-50µg/ml.

      What is the amino acid sequence of BD4 Protein?
      QSINNPITCL TKGGVCWGPC TGGFRQIGTC GLPRVRCCKK K.

      What applications can BD4 Protein be used in?
      BD4 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BD4 Protein?
      The endotoxin level is minimal, BD4 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.

    Bd 4 Rat
  • View Data Sheet

    Name :

    ERH Human

    Description:

    Enhancer of Rudimentary Human Recombinant

    Enhancer of rudimentary homolog, ERH, DROER, FLJ27340.

    Product # :

    PRO-121

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    Description

    ERH Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids (1-104 a.a.) and having a molecular mass of 14.6kDa. The ERH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Enhancer of rudimentary homolog (ERH) is a ubiquitously expressed transcriptional coregulator which is highly conserved among eukaryotes. ERH may have a role in cell cycle regulation and pyrimidine biosynthesis. ERH has two casein kinase II phosphorylation sites which are thought to upset the ability of ERH to dimerize.

    • Synonyms

      Enhancer of rudimentary homolog, ERH, DROER, FLJ27340.

    • 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 MGSMSHTILL VQPTKRPEGR TYADYESVNE CMEGVCKMYE EHLKRMNPNS PSITYDISQL FDFIDDLADL SCLVYRADTQ TYQPYNKDWI KEKIYVLLRR QAQQAGK.

    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.

    Erh Human
  • View Data Sheet

    Name :

    TFF3 Human

    Description:

    Trefoil Factor-3 Human Recombinant

    TFF-3, ITF, TFI, HITF, hP1.B, TFF3, Trefoil factor 3, Intestinal trefoil factor.

    Product # :

    CYT-005

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    Description

    TFF-3 Human Recombinant produced in E.Coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 59 amino acid chains which includes a 40 amino acid trefoil motif containing 3 conserved interamolecular disulfide bonds and having a total molecular mass of 13.2kDa. TFF-3 Human Recombinant 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 RP-HPLC and SDS-PAGE analysis.

    Biological Activity

    The ED50 as determined by a chemotaxis bioassay using human MCF-7 cells is less than 10µg/ml, corresponding to a specific activity of > 100IU/mg.

    More Info

    • Introduction

      Proteins of the TFF family are characterized by obtaining a minimum of 1 copy of the trefoil motif, a 40-amino acid domain that contains 3 conserved disulfides. Trefoil Factors are stable secretory proteins expressed in gastrointestinal mucosa which protect the mucosa from insults, stabilize the mucus layer and affect healing of the epithelium.TFF2 inhibits gastric acid motility & secretion. TFF2 stabilizes glycoproteins in the mucus gel through interactions with carbohydrate side chains. TFF3 induces ciliogenesis and promotes airway epithelial ciliated cell differentiation, relatively through an epidermal growth factor receptor-dependent pathway. TFF3 overexpression is crucial for progression in mouse and human hepatocellular carcinogenesis. TFF-3 is normally expressed in hepatocellular carcinoma and its expression associates with tumor grade.

    • Synonyms

      TFF-3, ITF, TFI, HITF, hP1.B, TFF3, Trefoil factor 3, Intestinal trefoil factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TFF3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TFF3 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 TFF3 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      EEYVGLSANQ CAVPAKDRVD CGYPHVTPKE CNNRGCCFDS RIPGVPWCFK PLQEAECTF.

    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.

    Tff3 Human
  • View Data Sheet

    Name :

    pHGF Porcine

    Description:

    Hepatocyte promoting Growth Factor Porcine

    Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF, pHGF.

    Product # :

    CYT-522

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    Description

    Hepatocyte Growth Factor porcine is extracted from pig liver.The HGF is purified by proprietary chromatographic techniques.

    Source

    Pig Liver.

    Formulation

    The sterile protein powder is 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

      Hepatocyte Growth Factor (HGF) is a multifunctional growth factor which regulates both cell growth and cell motility. It exerts a strong mitogenic effect on hepatocytes and primary epithelial cells. HGF synergizes with Interleukin-3and GM-CSFto stimulate colony formation of hematopoietic progenitor cells in vitro and may, therefore, also modulate hematopoiesis.

    • Synonyms

      Scatter Factor (SF), Hepatopoietin (HPTA), HGF, HGFB, F-TCF, pHGF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

      What is the source or expression system of PHGF PORCINE Protein?
      Pig Liver.

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

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

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

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

    Hgf Porcine
  • View Data Sheet

    Name :

    CD163 Porcine

    Description:

    CD163 Porcine Recombinant

    CD-163, Hemoglobin scavenger receptor, macrophage-associated antigen, M130, sCD163, CD163, MM130.

    Product # :

    PRO-856

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    Description

    CD163 Porcine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 805 amino acids and having a molecular mass of 87kDa.The CD163 is fused to an 8 amino acid His Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein was lyophilized from a 0.2µm filtered concentrated solution in 1×PBS, pH 7.4, containing 4M Urea.

    Purity

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

    More Info

    • Introduction

      CD163 is an acute phase-regulated receptor which participates in the removal and endocytosis of hemoglobin/haptoglobin complexes by macrophages and thus keeps tissues from free hemoglobin-mediated oxidative damage. Furthermore, CD163 partakes in the uptake and recycling of iron, through endocytosis of hemoglobin/haptoglobin and ensuing breakdown of heme. In addition, CD163 binds hemoglobin/haptoglobin complexes in a calcium-dependent and pH-dependent way. CD163 demonstrates greater affinity for complexes of hemoglobin and multimeric haptoglobin of HP-1F phenotype than for complexes of hemoglobin and dimeric haptoglobin of HP-1S phenotype. Moreover, CD163 stimulates a cascade of intracellular signals which involves tyrosine kinase-dependent calcium recruitment, inositol triphosphate formation and secretion of IL-6 & CSF-1.

    • Synonyms

      CD-163, Hemoglobin scavenger receptor, macrophage-associated antigen, M130, sCD163, CD163, MM130.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CD163 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD163 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 CD163 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MDKLRMVLHE NSGSADLKLR VVDGVTECSG RLEVKFQGEW GTICDDGWDS DDAAVACKQL GCPTAVTAIG RVNASEGTGH IWLDSVSCHG HESALWQCRH HEWGKHYCNH NEDAGVTCSD GSDLELRLKG GGSHCAGTVE VEIQKLVGKV CDRSWGLKEA DVVCRQLGCG SALKTSYQVY SKTKATNTWL FVSSCNGNET SLWDCKNWQW GGLSCDHYDE AKITCSAHRK PRLVGGDIPC SGRVEVQHGD TWGTVCDSDF SLEAASVLCR ELQCGTVVSL LGGAHFGEGS GQIWAEEFQC EGHESHLSLC PVAPRPDGTC SHSRDVGVVC SRYTQIRLVN GKTPCEGRVE LNILGSWGSL CNSHWDMEDA HVLCQQLKCG VALSIPGGAP FGKGSEQVWR HMFHCTGTEK HMGDCSVTAL GASLCSSGQV ASVICSGNQS QTLSPCNSSS SDPSSSIISE ENGVACIGSG QLRLVDGGGR CAGRVEVYHE GSWGTICDDS WDLNDAHVVC KQLSCGWAIN ATGSAHFGEG TGPIWLDEIN CNGKESHIWQ CHSHGWGRHN CRHKEDAGVI CSEFMSLRLI SENSRETCAG RLEVFYNGAW GSVGKNSMSP ATVGVVCRQL GCADRGDISP ASSDKTVSRH MWVDNVQCPK GPDTLWQCPS SPWKKRLASP SEETWITCAN KIRLQEGNTN CSGRVEIWYG GSWGTVCDDS WDLEDAQVVC RQLGCGSALE AGKEAAFGQG TGPIWLNEVK CKGNETSLWD CPARSWGHSD CGHKEDAAVT CSEIAKSRES LHATGRSHHH HHHHH.

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    Cd163 Porcine
  • View Data Sheet

    Name :

    Pleiotrophin Human, His

    Description:

    Pleiotrophin Human Recombinant, His Tag

    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-451

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    Description

    Pleiotrophin Human Recombinant contains His-Tagged Fusion Protein, produced in E. coli, its molecular weight is 17.3 kDa protein containing 136 amino acid residues of the OSF-1 human and 16 additional amino acid residues - HisTag, thrombin cleavage site (underlined).

    Source

    Escherichia Coli.

    Formulation

    Filtered and lyophilized from 0.5 mg/ml in 0.1M phosphate buffer and 0.1M NaCl, pH 7.2.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • 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

      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

      Add PBS pH 7.2 and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MKHHHHHHHM LVPRGSGKKE KPEKKVKKSD CGEWQWSVCV PTSGDCGLGT REGTRTGAEC KQTMKTQRCK IPCNWKKQFG AECKYQFQAW GECDLNTALK TRTGSLKRAL HNAECQKTVT ISKPCGKLTK PKPQAESKKK KKEGKKQEKM LD.

    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.

    Pleiotrophin Human
  • View Data Sheet

    Name :

    PPIH Human

    Description:

    Cyclophilin-H Human Recombinant

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

    Product # :

    ENZ-379

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    Description

    PPIH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 177 amino acids (1-177) and having a molecular mass of 19.2 kDa. PPIH is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1 mg/ml solution containing 1x PBS pH-7.4 10% glycerol.

    Purity

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

    Biological Activity

    Specific activity is > 220 nmoles/min/mg, and is defined as the amount of enzyme that cleaves 1umole of suc-AAFP-pNA per minute at 25C in Tris-Hcl pH8.0 using chymotrypsin.

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MAVANSSPVN PVVFFDVSIG GQEVGRMKIE LFADVVPKTA ENFRQFCTGEFRKDGVPIGY KGSTFHRVIK DFMIQGGDFV NGDGTGVASI YRGPFADENF KLRHSAPGLL SMANSGPSTN GCQFFITCSK CDWLDGKHVV FGKIIDGLLV MRKIENVPTG PNNKPKLPVV ISQCGEM.

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

    Ppih Human
  • View Data Sheet

    Name :

    LIF Mouse

    Description:

    Leukemia Inhibitory Factor Mouse Recombinant

    CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    Product # :

    CYT-645

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    Description

    Leukemia Inhibitory Factor (LIF) Murine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 20mM Phosphate buffer pH-7.4 and 0.02% Tween-20.

    Purity

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

    Biological Activity

    Activity of murine LIF was determined by the M1 cell differentiation assay which was found to be < 0.01 ng/ml, corresponding to a specific activity of 100,000,000 IU/mg.
    A standard of 50 Units is defined as the concentration of mouse LIF in 1.0 mL of tissue culture medium that induces the differentiation of 50% of M1 colonies.

    More Info

    • Introduction

      Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.

    • Synonyms

      CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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 Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MSPLPITPVNATCAIRHPCHGNLMNQIKNQLAQLNGSANALFISYYTAQGEPFP NNVEKLCAPNMTDFPSFHGNGTEKTKLVELYRMVAYLSASLTNITRDQKVLNP TAVSLQVKLNATIDVMRGLLSNVLCRLCNKYRVGHVDVPPVPDHSDKEAFQR KKLGCQLLGTYKQVISVVVQAF.

    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.

    Lif Mouse
  • View Data Sheet

    Name :

    WISP2 Human

    Description:

    WNT1 Inducible Signaling Pathway Protein 2 Human Recombinant

    WNT1 Inducible Signaling Pathway Protein 2, Connective Tissue Growth Factor-Related Protein 58, Connective Tissue Growth Factor-Like Protein, CCN Family Member 5, CTGF-L, CT58, CCN5, WISP-2, CTGFL, WISP2.

    Product # :

    CYT-970

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    Description

    WISP2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing a total of 228 amino acids and having a molecular mass of 24.4kDa.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a sterile (0.2µm) filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      WNT1-inducible-signaling pathway protein 2 (WISP2) belongs to the WNT1 inducible signaling pathway (WISP) protein subfamily, which belongs to the connective tissue growth factor (CTGF) family. The CTGF family members are characterized by 4 conserved cysteine-rich domains: insulin-like growth factor-binding domain, von Willebrand factor type C module, thrombospondin domain and C-terminal cystine knot-like (CT) domain. WISP2 protein lacks the CT domain which is implicated in dimerization binding. WISP2 is possibly involved in bone remodeling. WISP2 is expressed in primary osteoblasts and fibroblasts. WISP2 stimulates osteoblast adhesion and inhibits osteocalcin production. WISP2 expression in colon tumors is reduced while the other 2 WISP members are overexpressed in colon tumors. WISP2 may play an imperative role in modulating bone turnover.

    • Synonyms

      WNT1 Inducible Signaling Pathway Protein 2, Connective Tissue Growth Factor-Related Protein 58, Connective Tissue Growth Factor-Like Protein, CCN Family Member 5, CTGF-L, CT58, CCN5, WISP-2, CTGFL, WISP2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized WISP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution WISP-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 WISP-2 in sterile 10mM acetic acidnot less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MQLCPTPCTC PWPPPRCPLG VPLVLDGCGC CRVCARRLGE PCDQLHVCDA SQGLVCQPGA GPGGRGALCL LAEDDSSCEV NGRLYREGET FQPHCSIRCR CEDGGFTCVP LCSEDVRLPS WDCPHPRRVE VLGKCCPEWV CGQGGGLGTQ PLPAQGPQFS GLVSSLPPGV PCPEWSTAWG PCSTTCGLGM ATRVSNQNRF CRLETQRRLC LSRPCPPSRG RSPQNSAF.

    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.

    Wisp2 Human
  • View Data Sheet

    Name :

    ZNF32 Human

    Description:

    Zinc Finger Protein 32 Human Recombinant

    KOX30, Zinc finger protein 32, C2H2-546, Zinc finger protein KOX30, ZNF32.

    Product # :

    PRO-1983

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    Description

    ZNF32 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 296 amino acids (1-273 a.a) and having a molecular mass of 33.4kDa. ZNF32 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ZNF32 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Zinc Finger Protein 32 (ZNF32) is a part of the krueppel C2H2-type zinc-finger protein family. ZNF32 which contains seven C2H2-type zinc fingers takes part in transcriptional regulation.

    • Synonyms

      KOX30, Zinc finger protein 32, C2H2-546, Zinc finger protein KOX30, ZNF32.

    • 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 MGSMFGFPTA TLLDCHGRYA QNVAFFNVMT EAHHKYDHSE ATGSSSWDIQ NSFRREKLEQ KSPDSKTLQE DSPGVRQRVY ECQECGKSFR QKGSLTLHER IHTGQKPFEC THCGKSFRAK GNLVTHQRIH TGEKPYQCKE CGKSFSQRGS LAVHERLHTG QKPYECAICQ RSFRNQSNLA VHRRVHSGEK PYRCDQCGKA FSQKGSLIVH IRVHTGLKPY ACTQCRKSFH TRGNCILHGK IHTGETPYLC GQCGKSFTQR GSLAVHQRSC SQRLTL.

    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.

    Znf32 Human
  • View Data Sheet

    Name :

    SIRPA Human

    Description:

    Signal-Regulatory Protein Alpha Human Recombinant

    Signal-Regulatory Protein Alpha, SHPS1, CD172 Antigen-Like Family Member A, Inhibitory Receptor SHPS-1, Macrophage Fusion Receptor, PTPNS1, SIRP, P84, BIT, MFR, Brain-Immunoglobulin-Like Molecule With Tyrosine-Based Activation Motifs, Brain Ig-Like Molecule With Tyrosine-Based Activation Motifs, Protein Tyrosine Phosphatase, Non-Receptor Type Substrate 1, Tyrosine-Protein Phosphatase Non-Receptor Type Substrate 1, Tyrosine Phosphatase SHP Substrate 1, Signal-Regulatory Protein Alpha-1 , ignal-Regulatory Protein Alpha-2, Signal-Regulatory Protein Alpha-3, SHP Substrate 1, CD172a Antigen, Myd-1 Antigen, MyD-1 Antigen, Sirp-Alpha-1, Sirp-Alpha-2, Sirp-Alpha-3, CD172A, SHPS-1, MYD-1, MYD1, Tyrosine-protein phosphatase non-receptor type substrate 1.

    Product # :

    PRO-2080

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    SIRPA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 370 amino acids (27-373 a.a) and having a molecular mass of 40.4kDa. SIRPA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SIRPA protein solution (0.5mg/ml) containing PBS buffer (pH 7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as theimmunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which areinvolved in the negative regulation of receptor tyrosine kinase-coupled signaling processes. SIRPA can bephosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part insignal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand for SIRPA.

    • Synonyms

      Signal-Regulatory Protein Alpha, SHPS1, CD172 Antigen-Like Family Member A, Inhibitory Receptor SHPS-1, Macrophage Fusion Receptor, PTPNS1, SIRP, P84, BIT, MFR, Brain-Immunoglobulin-Like Molecule With Tyrosine-Based Activation Motifs, Brain Ig-Like Molecule With Tyrosine-Based Activation Motifs, Protein Tyrosine Phosphatase, Non-Receptor Type Substrate 1, Tyrosine-Protein Phosphatase Non-Receptor Type Substrate 1, Tyrosine Phosphatase SHP Substrate 1, Signal-Regulatory Protein Alpha-1 , ignal-Regulatory Protein Alpha-2, Signal-Regulatory Protein Alpha-3, SHP Substrate 1, CD172a Antigen, Myd-1 Antigen, MyD-1 Antigen, Sirp-Alpha-1, Sirp-Alpha-2, Sirp-Alpha-3, CD172A, SHPS-1, MYD-1, MYD1, Tyrosine-protein phosphatase non-receptor type substrate 1.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSGVAGEEE LQVIQPDKSV LVAAGETATL RCTATSLIPV GPIQWFRGAG PGRELIYNQK EGHFPRVTTV SDLTKRNNMD FSIRIGNITP ADAGTYYCVK FRKGSPDDVE FKSGAGTELS VRAKPSAPVV SGPAARATPQ HTVSFTCESH GFSPRDITLK WFKNGNELSD FQTNVDPVGE SVSYSIHSTA KVVLTREDVH SQVICEVAHV TLQGDPLRGT ANLSETIRVP PTLEVTQQPV RAENQVNVTC QVRKFYPQRL QLTWLENGNV SRTETASTVT ENKDGTYNWM SWLLVNVSAH RDDVKLTCQV EHDGQPAVSK SHDLKVSAHP KEQGSNTAAE NTGSNERNIY.

    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.

    Sirpa Human
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