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1000 results found for “profilin”
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Name :
MoeXDescription:
Mycobacterium Tuberculosis MoeX Recombinant
Product # :
PRO-1919Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Mycobacterium Tuberculosis MoeX produced in E.Coli is a single, non-glycosylated, polypeptide chain having a molecular mass of 38 kDa. The MoeX is fused to a His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MoeX protein solution 0.75mg/ml contains 1xPBS, 25mM arginine and 0.02% NaN3.
Purity
Protein is >95% pure as determined by 12% PAGE (coomassie staining).
More Info
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Physical Appearance
Sterile Filtered clear solution.
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Stability
MoeX Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Der F1Description:
Der F1 Mosaic Protein Recombinant
Product # :
ALR-004Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
The E.Coli derived recombinant protein contains the Dermatophagoides farina Der F1 full length protein (a.a. 1-320) and fused to a 6 His Tag at C-terminus, having a total Mw of 36kDa, pI 5.88.
Source
E.Coli.
Formulation
60mM NaCl, 50mM Tris-HCl pH 8.0 and 1.2M Urea.
Purity
Protein is >95% pure as determined by 10% PAGE (coomassie staining) and RP-HPLC.
More Info
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Introduction
DERF1 is a thiol protease that hydrolyzes proteins, with a preference for Phe or basic residues. DERF1 is a C1 peptidase family member. DERF1 has extensive endopeptidase specificity. DERF1 causes an allergic reaction in humans. Common symptoms of mite allergy are bronchial asthma, allergic rhinitis and conjunctivitis.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Der F1 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Purification Method
Purified by proprietary chromatographic technique.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ITAC (63-87) HumanDescription:
ITAC (63-87 a.a.) Human Recombinant
ITAC, I-TAC, CXCL-11, CXCL11.
Product # :
CHM-049Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The I-TAC Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The I-TAC His-Tagged Fusion Protein, produced in E. coli, is a 9kDa protein containing 25 amino acid residues of the I-TACHuman, 63-87 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
ITAC, I-TAC, CXCL-11, CXCL11.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized I-TAC 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.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Background
I-TAC is a small cytokine belongs to the CXC chemokinen family which also called inducible T-cell alpha chemoattractant and IP-9. I-TAC is expressed mainly in peripheral blood leukocytes, liver and pancreas with moderate levels in spleen, thymus and lung and low levels in small intestine, placenta and prostate. IFN-g and IFN-b induces strongly gene expression of I-TAC. The I-TAC chemokine elicits its effects on its target cells by interacting with the cell surface chemokine receptor CXCR3, with a higher affinity than do the other ligands for this receptor, CXCL9 and CXCL10.
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.
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Name :
PVR HumanDescription:
Poliovirus Receptor Human Recombinant
Poliovirus receptor, Nectin-like protein 5, NECL-5, CD155, PVR, PVS.
Product # :
PRO-2463Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PVR Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 331 amino acids (21-343 a.a.) and having a molecular mass of 36.1kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PVR is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PVR protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Poliovirus receptor, also known as PVR, is a Type I transmembrane glycoprotein which belongs to the immunoglobulin superfamily. PVR catalyzes a big structural modification in the virus which exposes membrane-binding protein chains. PVR regulates helper T cell differentiation as well as allergic diseases. PVR is expressed in many kinds of human cells and has various functions. PVR is potentially functional as a biomarker for cancer development as well as progression. PVR takes a vital part through both immunological & non-immunological mechanisms in pancreatic cancer.
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Synonyms
Poliovirus receptor, Nectin-like protein 5, NECL-5, CD155, PVR, PVS.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
WPPPGTGDVV VQAPTQVPGF LGDSVTLPCY LQVPNMEVTH VSQLTWARHG ESGSMAVFHQ TQGPSYSESK RLEFVAARLG AELRNASLRM FGLRVEDEGN YTCLFVTFPQ GSRSVDIWLR VLAKPQNTAE VQKVQLTGEP VPMARCVSTG GRPPAQITWH SDLGGMPNTS QVPGFLSGTV TVTSLWILVP SSQVDGKNVT CKVEHESFEK PQLLTVNLTV YYPPEVSISG YDNNWYLGQN EATLTCDARS NPEPTGYNWS TTMGPLPPFA VAQGAQLLIR PVDKPINTTL ICNVTNALGA RQAELTVQVK EGPPSEHSGM SRNLEHHHHH H
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
Protein A, 434 a.aDescription:
Staphylococcal Protein A 434 a.a Recombinant
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Product # :
PRO-686Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Staphylococcal Protein A produced in E.Coli is a non-glycosylated, Polypeptide chain containing 434 amino acids (37-469 a.a.) and having a molecular mass of 48.1 kDa. Recombinant Staphylococcal Protein A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Protein-A protein solution contains 20mM Tris-HCl, pH-8 and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Protein A is a cell wall protein deriving from Staphylococcus aureus which exhibits unique binding properties for IgG from a variety of mammalian species and for some IgM and IgA as well. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. It couples to a wide variety of reporter molecules including fluorescent dyes, enzyme markers, biotin, colloidal gold and radioactive iodine without affecting the antibody binding site. Recombinant Protein A was developed to increase the specificity of the molecule for IgG and is widely used both in research and bioprocessing. The recombinant protein A is produced by expressing a modified protein A gene in E.coli. A specific purification process with strict quality control was taken to get the recombinant protein A with the purity of more than 98% , no human IgG affinity step is used during validated fermentation and purification and devoid of bacterial contaminant found normally in native Protein A. (Free of Staphylococcus endotoxins and hemolysin).
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Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MAQHDEAQQN AFYQVLNMPN LNADQRNGFI QSLKDDPSQS ANVLGEAQKL NDSQAPKADA QQNNFNKDQQ SAFYEILNMP NLNEAQRNGFIQSLKDDPSQ STNVLGEAKK LNESQAPKAD NNFNKEQQNA FYEILNMPNL NEEQRNGFIQ SLKDDPSQSA NLLSEAKKLN ESQAPKADNK
FNKEQQNAFY EILHLPNLNE EQRNGFIQSL KDDPSQSANL LAEAKKLNDA QAPKADNKFN KEQQNAFYEI LHLPNLTEEQ RNGFIQSLKDDPSVSKEILA EAKKLNDAQA PKEEDNNKPG KEDNNKPGKE DNNKPGKEDG NKPGKEDNKK PGKEDNKKPG KEDNKKPGKE DGNKPGKEDN
KKPGKEDGNG VHVVKPGDTV NDIAKANGTT ADKIAADNKL ADKNMIKPGQ ELVVDKKQPA NHADANKAQA LPET.
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.
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Name :
HIV-1 gp41, BiotinDescription:
HIV-1 gp41 Recombinant, Biotin labeled
Product # :
HIV-117Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HIV-1 gp41 Biotin labeled is a non-glycosylated polypeptide chain, containing 288 amino acids (466-753 a.a.) and having an Mw of 32kDa. HIV1 gp41 biotin labeled is fused to an 114kDa beta-galactosidase tag at N-terminus having a total Mw of 146kDa.
Source
Escherichia Coli.
Formulation
1mg/ml in 20mM Tris-HCl pH-8, 10mM B-ME and 8M urea.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Human immunodeficiency virus (HIV) is a retrovirusthat can lead to a condition in which the immune systembegins to fail, leading to opportunistic infections. HIV primarily infects vital cells in the humanimmune systemsuch as helper T cells(specifically CD4+ T cells), macrophagesand dendritic cells. HIV infection leads to low levels of CD4+ T cells through three main mechanisms: firstly, direct viral killing of infected cells; secondly, increased rates of apoptosisin infected cells; and thirdly, killing of infected CD4+ T cells by CD8 cytotoxic lymphocytesthat recognize infected cells. When CD4+ T cell numbers decline below a critical level, cell-mediated immunityis lost, and the body becomes progressively more susceptible to opportunistic infections. HIV was classified as a member of the genus Lentivirus, part of the family of Retroviridae. Lentiviruses have many common morphologies and biological properties. Many species are infected by lentiviruses, which are characteristically responsible for long-duration illnesses with a long incubation period. Lentiviruses are transmitted as single-stranded, positive-sense, enveloped RNA viruses. Upon entry of the target cell, the viral RNA genomeis converted to double-stranded DNAby a virally encoded reverse transcriptasethat is present in the virus particle. This viral DNA is then integrated into the cellular DNA by a virally encoded integraseso that the genome can be transcribed. Once the virus has infected the cell, two pathways are possible: either the virus becomes latentand the infected cell continues to function, or the virus becomes active and replicates, and a large number of virus particles are liberated that can then infect other cells.
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Physical Appearance
Sterile filtered colorless clear solution.
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Stability
HIV-1 gp41 Biotin although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
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Specificity
Reacts with Human HIV positive serum.
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.
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Name :
ATF BovineDescription:
Apo Transferrin Bovine
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
Product # :
PRO-511Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bovine Apo Transferrin is a glycoprotein of approximately 77kDa.
Source
Bovine Serum.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
Bovine Transferrin is a crucial component for the cultivation of mammalian cells in- vitro. Bovine Transferrin is Critical for long-term cells growth in-vitro. Bovine Transferrin is used as detoxificant in media by binding contaminating metal ions. Bovine Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Bovine Transferrin are Molecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells. -
Synonyms
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.
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Physical Appearance
Sterile Filtered off-white lyophilized (freeze-dried) powder.
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Stability
Store the lyophilized Apo Transferrin between 2-8°C, do not freeze.
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Solubility
It is recommended to reconstitute the lyophilized Apo Transferrin in sterile 18MΩ-cm H2O not less than 1gr/30ml in 20min. at 20-25C.
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Iron Content
The Iron content was estimated by ICP-OES and was found to be less than 40 ppm.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SAA EquineDescription:
Serum Amyloid A (APO-SAA) Equine Recombinant
Product # :
CYT-1222Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SAA Equine produced in E.coli is a single, non-glycosylated polypeptide chain (1-110 a.a) containing 120 a.a and having a molecular mass of 13,580 Dalton. SAA s fused with a 10 amino acids affinity tag at N-Terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SAA was lyophilized from 0.01M HCl (pH 2.0).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized SAA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Serum Amyloid A (APO-SAA) 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.
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Solubility
It is recommended to reconstitute the lyophilized SAA in 0.01M HCl (pH 2.0) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Elevated SAA levels serve as sensitive markers for various inflammatory disorders, including infections, autoimmune diseases, and cancer. SAA assays, often utilizing recombinant SAA proteins, are invaluable in clinical diagnostics, aiding in disease monitoring and treatment evaluation. Moreover, the targeted modulation of SAA activities presents novel therapeutic strategies, offering potential interventions in conditions characterized by excessive inflammation.
SAA Recombinant Protein, as a representative of the intricate SAA family, embodies the complexities of inflammation, immune regulation, and lipid metabolism. Its versatile roles in health and disease underscore its significance in biology and medicine. By unraveling the molecular intricacies of SAA, scientists pave the way for innovative diagnostic methods, therapeutic interventions, and a deeper understanding of the intricate interplay between inflammation and various physiological processes. This research not only illuminates the multifaceted nature of SAA but also holds the promise of transformative advancements in both clinical practice and scientific discovery.
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.
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Name :
TnT HumanDescription:
Cardiac Troponin T Human
Troponin T cardiac muscle, TnTc, Cardiac muscle troponin T, cTnT, TNNT2, CMH2, CMPD2, MGC3889.
Product # :
PRO-342Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Human Cardiac Troponin T produced from Human Cardiac Tissue, having a molecular weight of approximately 35 kDa.
The Cardiac troponin-T is Immunogen for troponin biochemical, antibody production and immunochemical studies.
Source
Human skeletal muscle.
Formulation
Human Cardiac Troponin was lyophilized in 0.01 M HCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Troponin-T is one of three subunits that form the troponin complex of the thin filaments of striated muscle, it regulates muscle contraction in response to alterations in intracellular calcium ion concentration. TnTc is expressed only in the heart and has proved to be a specific biomarker for heart disease.
Mutations in TNNT2 are associated with familial hypertrophic cardiomyopathy as well as with dilated cardiomyopathy.
Alternative splicing results in many tissue-specific isoforms. -
Synonyms
Troponin T cardiac muscle, TnTc, Cardiac muscle troponin T, cTnT, TNNT2, CMH2, CMPD2, MGC3889.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TnT although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cardiac Troponin T 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.
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Solubility
It is recommended to reconstitute the lyophilized TnT with urea /Tris buffer (20mM Tris, pH 7.5, 5 mM EDTA, 7 M urea and 15 mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Human Virus Test
Blood sample from the tissue donor was tested and found negative for HBsAg, HIV-1 and HIV-2 antibodies, HCV, and syphilis.
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.
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Name :
IL 3 Human, HisDescription:
Interleukin-3 Human Recombinant, His Tag
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
Product # :
CYT-482Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Interleukin-3 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 154 amino acids fragment (20-152) and having a total molecular mass of 17.3kDa and fused with a 20 aa N-terminal His tag. The IL3 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Interleukin-3 His (1mg/ml) is supplied in 20mM Tris-HCl buffer (pH 8.0), 0.2mM PMSF and 10% glycerol.
Purity
Greater than 90.0% as determined by analysis by SDS-PAGE.
Biological Activity
The ED50 for this effect is <0.53ng/ml. Measured in a cell proliferation assay using TF1 human erythroleukemic cells.More Info
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Introduction
Interleukin-3 is a pleiotropic cytokine produced primarily by activated T cells. IL-3 is thought to function via specific cell surface receptors to stimulate the proliferation, differentiation and survival of haematopoietic cell lines. IL-3 has also been shown to affect the functional activity of a variety of other cell types including mast cells, eosinophils, megakaryocytes and basophils.
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Synonyms
MCGF (Mast cell growth factor), Multi-CSF, HCGF, P-cell stimulation factor, IL-3, MGC79398, MGC79399.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAPMTQTTSL KTSWVNCSNM IDEIITHLKQ PPLPLLDFNN LNGEDQDILM ENNLRRPNLE AFNRAVKSLQ NASAIESILK NLLPCLPLAT AAPTRHPIHI KDGDWNEFRR KLTFYLKTLE NAQAQQTTLS LAIF.
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.
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Name :
SPP1 MouseDescription:
Osteopontin 1 Mouse Recombinant
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1
Product # :
CYT-1201Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SPP1 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 287 amino acids (17-294 a.a) and having a molecular mass of 31.8kDa.SPP1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The SPP1 solution (0.25mg/1ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Measured by the ability of the immobilized protein to support the adhesion of HEK293 HEK cells when the cells are added to mouse SPP1 coated plates. The ED50 range is ≤ 1.5 ug/ml.
More Info
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Introduction
Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction. Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases.
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Synonyms
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
DGSLPVKVTD SGSSEEKLYS LHPDPIATWL VPDPSQKQNL LAPQNAVSSE EKDDFKQETL PSNSNESHDH MDDDDDDDDD DGDHAESEDS VDSDESDESH HSDESDETVT ASTQADTFTP IVPTVDVPNG RGDSLAYGLR SKSRSFQVSD EQYPDATDED LTSHMKSGES KESLDVIPVA QLLSMPSDQD NNGKGSHESS QLDEPSLETH RLEHSKESQE SADQSDVIDS QASSKASLEH QSHKFHSHKD KLVLDPKSKE DDRYLKFRIS HELESSSSEV NHHHHHH
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.
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Name :
DGCR6L HumanDescription:
DiGeorge Syndrome Critical Region Gene 6-Like Human Recombinant
Protein DGCR6L, DiGeorge syndrome critical region 6-like protein, DGCR6L.
Product # :
PRO-1454Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
DGCR6L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 243 amino acids (1-220 a.a) and having a molecular mass of 27.3kDa.DGCR6L is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
DGCR6L protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 50% glycerol, 1mM DTT and 250mM Imidazole.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
DiGeorge syndrome critical region 6-like protein (DGCR6L) shares homology with the Drosophila gonadal protein, it is expressed in gonadal tissues and germ cells, and with the human laminin gamma-1 chain which functions in cell attachment and migration. DGCR6L is located in a region of chromosome 22 involved in the DiGeorge syndrome, one aspect of a wider collection of anomalies referred to as the CATCH 22 syndrome. Moreover, it is one of two functional genes encoding nearly identical proteins which have analogous expression patterns.
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Synonyms
Protein DGCR6L, DiGeorge syndrome critical region 6-like protein, DGCR6L.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMERYAAA LEEVADGARQ QERHYQLLSA LQSLVKELPS SFQQRLSYTT LSDLALALLD GTVFEIVQGL LEIQHLTEKS LYNQRLRLQN EHRVLRQALR QKHQEAQQAC RPHNLPVVQA AQQRELEAVE HRIREEQRAM DQKIILELDR KVADQQSTLE KAGVAGFYVT TNPQELMLQM NLLELIRKLQ QRGCRAGNAA LGLGGPWQSP AAQCDQKGSP VPP.
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.
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Name :
EFNA5 Human, ActiveDescription:
Ephrin A5 Human Recombinant, Active
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
Product # :
PRO-2816Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
EFNA5 Human Recombinant is a single, glycosylated, polypeptide chain (21-203 a.a) containing a total of 422 amino acids and having a molecular mass of 48.1 kDa. EFNA5 is fused to a 239 a.a hIgG-His-Tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The EFNA5 solution (0.5mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 60 ng/ml measured by its binding ability in a functional ELISA with Mouse EphA3 (CAT# pro-2817).
More Info
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Synonyms
EFNA5, AF1, EFL5, EPLG7, GLC1M, LERK7, RAGS, Ephrin-A5, AL-1, EPH-related receptor tyrosine kinase ligand 7.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
QDPGSKAVAD RYAVYWNSSN PRFQRGDYHI DVCINDYLDV FCPHYEDSVP EDKTERYVLY MVNFDGYSAC DHTSKGFKRW ECNRPHSPNG PLKFSEKFQL FTPFSLGFEF RPGREYFYIS SAIPDNGRRS CLKLKVFVRP TNSCMKTIGV HDRVFDVNDK VENSLEPADD TVHESAEPSR GENLEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.
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Background
EFNA5 functions through contact-mediated signaling, which can result in either forward signaling (through Eph receptors) or reverse signaling (through ephrins themselves). These signaling pathways regulate various cellular processes such as migration, adhesion, and proliferation. Disruptions or alterations in EFNA5 signaling have been implicated in neurodevelopmental disorders, cancer metastasis, and angiogenesis, highlighting the importance of understanding this protein's roles at a molecular level.
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.
- View Data Sheet
Name :
TPM2 HumanDescription:
Tropomyosin-2 Human Recombinant
Tropomyosin 2 (beta), DA1, TMSB, DA2B, AMCD1, NEM4, Arthrogryposis Multiplex Congenital Distal-Type 1, beta-Tropomyosin.
Product # :
PRO-069Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TPM2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (1-284a.a.) and having a molecular mass of 35.1kDa(molecular weight on SDS-PAGE will appear higher).TPM2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TPM2 protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 100mM NaCl and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Tropomyosin beta chain isoform 2 is affiliate to the actin filament binding protein family which primarily expressed in slow, type 1 muscle fibers. Mutations in TPM2 can change the expression of other sarcomeric tropomyosin proteins, and cause cap disease, nemaline myopathy and distal arthrogryposis syndromes.
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Synonyms
Tropomyosin 2 (beta), DA1, TMSB, DA2B, AMCD1, NEM4, Arthrogryposis Multiplex Congenital Distal-Type 1, beta-Tropomyosin.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MDAIKKKMQM LKLDKENAID RAEQAEADKK QAEDRCKQLE EEQQALQKKL KGTEDEVEKY SESVKEAQEK LEQAEKKATD AEADVASLNR RIQLVEEELD RAQERLATAL QKLEEAEKAA DESERGMKVI ENRAMKDEEK MELQEMQLKE AKHIAEDSDR KYEEVARKLV ILEGELERSE ERAEVAESRA RQLEEELRTM DQALKSLMAS EEEYSTKEDK YEEEIKLLEE KLKEAETRAE FAERSVAKLE KTIDDLEETL ASAKEENVEI HQTLDQTLLE LNNL.
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.
- View Data Sheet
Name :
Collagen-IV BovineDescription:
Bovine Collagen-IV
Product # :
PRO-2678Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Bovine Collagen-IV is a natural protein purified from bovine placenta. Collagen-IV is purified by proprietary chromatographic techniques.
Source
Bovine placenta.
Formulation
Collagen-IV was lyophilized without additives.
Purity
> 90.0% .
More Info
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Introduction
Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Collagen-IV although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Collagen-IV should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Collagen-IV in 20 mM acetic acid not less than 1mg/ml, which can then be further diluted to other aqueous solutions.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
Mouse OX40LDescription:
OX40 Ligand Mouse Recombinant
Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l
Product # :
CYT-1191Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
OX40L Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 157 amino acids (51-198 aa) and having a molecular mass of 17.7kDa.OX40L is fused to a 6 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
The OX40L solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Determined by its binding ability in a functional ELISA with Human TNFRSF4 (CAT# cyt-1039).
More Info
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Introduction
OX40 Ligandis a part of the tumor necrosis factor (TNF)receptor family. OX40L receptor is OX40 which is expressed predominantly on activated CD4+ T cells.OX40 Ligandis expressed on various antigen-presenting cells such asmacrophages, DC2sand activated Blymphocytes. Expression of OX40 is momentary following engagement of T cell receptors. The ligation of OX40-OX40L stimulates proliferation anddifferentiation of activated B cells,increases immunoglobulin secretion and is also a sourceof survival signal for T cells and enables the development of memory T cells.
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Synonyms
Tumor necrosis factor ligand superfamily member 4, OX40 ligand, OX40L, OX-40L, CD252, Tnfsf4, Ox40l, Txgp1l, gp3, OX4, Ath-1, Ath1, CD134L, gp34, Tnlg2b, Txgp1l
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
ADPSSSPAKD PPIQRLRGAV TRCEDGQLFI SSYKNEYQTM EVQNNSVVIK CDGLYIIYLK GSFFQEVKID LHFREDHNPI SIPMLNDGRR IVFTVVASLA FKDKVYLTVN APDTLCEHLQ INDGELIVVQ LTPGYCAPEG SYHSTVNQVP LHHHHHH
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.
- View Data Sheet
Name :
CoV-2 3CLDescription:
Coronavirus 2019 3CL Protease Recombinant
Product # :
SARS-058Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Recombinant Coronavirus 2019 3CL Protease having a Mw of approximately 33.8 kDa was purified from E. coli. The CoV-2 3CL contains 306 amino acids and purified by proprietary chromatographic technique.
Source
Escherichia Coli.
Formulation
CoV-2 3CL solution contains 5 % Trehalose, 0.02 % Tween-20 and PBS, pH 7.4.
Purity
Protein is >98% pure as determined by SDS-PAGE and HPLC analyses.
Biological Activity
CoV-2 3CL is a cysteine protease that cleaves proteins with sequences including LQ(S/A/G). The cleavage takes c-terminal to the glutamine residue.
More Info
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Introduction
The SARS CoV-2 3CL protease (C30 Endopeptidase) derived from human SARS-CoV-2 is a C30-type cysteine protease situated in the NS3 segment. SARS CoV-2 3CL protease biological functionality is needed to process viral polyproteins to functional complete units. SARS CoV-2 3CL protease (main protease) is the core protease protein in CoV and corresponds to non-structural protein 5. SARS CoV-2 3CL cleaves the CoV polyprotein at 11 locations. SARS CoV-2 3CL protease has a cysteine-histidine catalytic dyad at its active site and cleaves a Gln–(Ser/Ala/Gly) peptide bond. SARS CoV-2 3CL protease at position P1 cleaves the bond between the glutamine and serine/alanine/glycine. SARS CoV-2 3CL protease is necessary in the processing of the CoV replicase polyprotein.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. CoV-2 3CL is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
SGFRKMAFPS GKVEGCMVQV TCGTTTLNGL WLDDVVYCPR HVICTSEDML NPNYEDLLIR KSNHNFLVQA GNVQLRVIGH SMQNCVLKLK VDTANPKTPK YKFVRIQPGQ TFSVLACYNG SPSGVYQCAM RPNFTIKGSF LNGSCGSVGF NIDYDCVSFC YMHHMELPTG VHAGTDLEGN FYGPFVDRQT AQAAGTDTTI TVNVLAWLYA AVINGDRWFL NRFTTTLNDF NLVAMKYNYE PLTQDHVDIL GPLSAQTGIA VLDMCASLKE LLQNGMNGRT ILGSALLEDE FTPFDVVRQC SGVTFQ
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.
- View Data Sheet
Name :
Insulin Human (20-110)Description:
Insulin (20-110 a.a) Human Recombinant
Product # :
CYT-1237Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
The Insulin Human is created as a recombinant protein with a 4kda N-terminal fusion of His Tag. The Insulin His-Tagged Fusion Protein, produced in E. coli, is a 13kDa protein containing 91 amino acid residues of the Insulin Human, 20-110 amino acids.
Source
Escherichia Coli.
Formulation
Each mg was lyophilized with 1xPBS, 0.4% SDS and 4mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized Insulin 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.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it on cell culture.
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Amino Acid Sequence
MALWMRLLPL LALLALWGPD PAAAFVNQHL CGSHLVEALY LVCGERGFFY TPKTRREAED LQVGQVELGG GPGAGSLQPL ALEGSLQKRG IVEQCCTSIC SLYQLENYCN
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Background
Insulin participates in the metabolism of carbohydrates, proteins and fats by regulating glucose homeostasis in the body. Insulin decreases blood glucose concentration. Insulin hormone facilitates the uptake of glucose into cells, mainly in muscle and fat tissues, and stimulates the liver to store glucose as glycogen. Insulin also inhibits the production of gluconeogenesis and promotes the synthesis of proteins and lipids. Insulin increases cell permeability to monosaccharides, fatty acids and amino acids. Insulin accelerates glycolysis, the pentose phosphate cycle and glycogen synthesis in liver.
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.
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Name :
HBsAg adwDescription:
Hepatitis B Surface Antigen, adw Recombinant
Product # :
HBS-872Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
HbsAg adw produced Pichia Pastoris, having a molecular weight of approximately 24.0 kDa as shown on SDS-PAGE.
Source
Pichia Pastoris.
Formulation
Sterile Filtered solution containing 20mM Phosphate Buffer, 154mM sodium chloride, pH 7.1.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
HBsAg is the surface antigenof the Hepatitis-B-Virus (HBV). The capsidof a virus has different surface proteins from the rest of the virus. The antigen is a protein that binds specifically on one of these surface proteins. It is commonly referred to as the Australian Antigen.
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Physical Appearance
Sterile Filtered pale solution.
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Stability
HBsAg Should be stored at 4°C.DO NOT FREEZE.
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.
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Name :
ProNGF HumanDescription:
Pro-Nerve Growth Factor Human Recombinant
Human Pro-NGF, ProNGF, NGFB.
Product # :
CYT-426Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Pro-NGF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 224 amino acids and having a molecular mass of 25 kDa.ProNGF Human Recombinant is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
ProNGF was lyophilized from a 0.2 μM filtered solution of 20m Tris-HCL, 0.5M NaCl, 5% Trehalose, 5% Mannitol. 0.01% Tween-80 and 1mM EDTA pH-8.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Human Pro-NGF, ProNGF, NGFB.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized ProNGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProNGF should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized ProNGF in distilled water to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
VCVLSRKAVRRA. -
Background
Pro-Nerve Growth Factor Human Recombinant: Unveiling its Potential in Neuroregulation and Disease Pathogenesis
Abstract:
Pro-Nerve Growth Factor (Pro-NGF) human recombinant is a crucial precursor protein involved in neuronal development, survival, and degenerative processes. This research paper aims to provide a comprehensive analysis of Pro-NGF, including its characteristics, processing mechanisms, and implications in neuroregulation and disease pathogenesis. Additionally, innovative methodologies for the production and manipulation of Pro-NGF human recombinant are proposed, highlighting its potential as a therapeutic target for neurological disorders and neurodegenerative diseases.
Introduction:
Neuroregulation and maintenance of neuronal health are intricate processes governed by a network of signaling molecules. Pro-NGF, the precursor form of Nerve Growth Factor (NGF), acts as a key player in neuronal development, synaptic plasticity, and cell survival. This paper delves into the distinctive features of Pro-NGF and presents novel approaches for the production and manipulation of Pro-NGF human recombinant, aiming to unravel its role in neuroregulation and disease pathogenesis.
Characteristics and Processing Mechanisms:
Pro-NGF is initially synthesized as an inactive precursor, requiring proteolytic cleavage for conversion into mature NGF. The processing of Pro-NGF involves the action of proteases, such as furin, and the formation of distinct protein complexes. The balance between Pro-NGF and mature NGF levels plays a critical role in modulating neuronal function and fate, influencing processes such as neuronal survival, axonal growth, and synaptic plasticity.
Production and Manipulation of Pro-NGF Human Recombinant:
Efficient production methodologies and manipulation strategies are crucial for studying the role of Pro-NGF in neuroregulation and disease pathogenesis. Recombinant protein expression systems, including mammalian cell culture and bacterial expression systems, have been employed to produce functional Pro-NGF human recombinant. Techniques such as mutagenesis, protein purification, and specific inhibitors targeting Pro-NGF processing pathways enable the manipulation of Pro-NGF levels and investigation of its downstream effects.
Implications in Neuroregulation and Disease Pathogenesis:
Pro-NGF human recombinant holds significant potential in understanding the intricate mechanisms underlying neuroregulation and disease pathogenesis. Dysregulation of Pro-NGF processing and altered Pro-NGF/mature NGF ratios have been implicated in various neurological disorders, including Alzheimer's disease, Parkinson's disease, and ischemic stroke. Manipulating Pro-NGF levels and the balance between its mature form may offer therapeutic strategies for modulating neurotrophic signaling and promoting neuronal health in these conditions.
Conclusion:
Pro-NGF human recombinant emerges as a key regulator in neuroregulation and disease pathogenesis, offering promising avenues for therapeutic intervention. Enhancing our understanding of Pro-NGF processing mechanisms and its downstream signaling cascades will provide valuable insights into neurodevelopment, neurodegeneration, and potential therapeutic strategies. Targeting Pro-NGF as a therapeutic intervention may hold immense promise in treating neurological disorders and promoting neuronal health.
What is the molecular weight / Mw of ProNGF Protein?
ProNGF Protein has a total Mw of 25kDa.
What is the source or expression system of ProNGF Protein?
Escherichia Coli.
What is the Purity of ProNGF Protein?
ProNGF Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of ProNGF Protein?
The biological functionality of ProNGF Protein will be determined in the future.
What is the amino acid sequence of ProNGF Protein?
MEPHSESNVPAGHTIPQAHWTKLQHSLDTALRRARSAPAAAIAARVAGQTRNI
TVDPRLFKKRRLRSPRVLFSTQPPREAADTQDLDFEVGGAAPFNRTHRSKRS
SSHPIFHRGEFSVCDSVSVWVGDKTTATDIKGKEVMVLGEVNINNSVFKQYFFET
KCRDPNPVDSGCRGIDSKHWNSYCTTTHTFVKALTMDGKQAAWRFIRIDTAC
VCVLSRKAVRRA
What applications can ProNGF Protein be used in?
Tissue Factor Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for ProNGF Protein?
The endotoxin level is minimal, ProNGF 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.
- View Data Sheet
Name :
Leptin HorseDescription:
Leptin Horse Recombinant
OB Protein, Obesity Protein, OBS, Obesity factor.
Product # :
CYT-504Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Leptin Horse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and having a molecular mass of 16 kDa.The Leptin is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.0045mM NaHCO3.
Purity
Greater than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Biological active as evidenced by inducing proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor.More Info
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Introduction
A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.
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Synonyms
OB Protein, Obesity Protein, OBS, Obesity factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leptin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin 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.
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Solubility
It is recommended to reconstitute the lyophilized Leptin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Gln.
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Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.1 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 calibrated solution of Leptin Horse 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.
- View Data Sheet
Name :
CRYAB HumanDescription:
Crystallin Alpha B Human Recombinant
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
Product # :
HSP-003Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
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- source
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Description
Recombinant CRYAB produced in E.Coli is a single,non-glycosylated polypeptide chain containing 175 amino acids and having a molecular mass of 20.1kDa. CRYAB is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CRYAB protein (1mg/ml) solution contains 20mM Tris-HCl buffer pH-7.5, 50mM NaCl and 1mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Alpha crystallins are composed of two gene products ; alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20). They act as molecular chaperones and hold them in in large soluble aggregates. These heterogeneous aggregates consist of 30-40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional function of a-crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-B is expressed widely in many tissues and organs and occurs in many neurological diseases.
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Synonyms
CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSWFDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHRKYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKK.
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.
- View Data Sheet
Name :
Prolactin OvineDescription:
Prolactin Ovine Recombinant
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
Product # :
CYT-240Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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Description
Prolactin Ovine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids and having a molecular mass of 23 kDa. The Prolactin n is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) solution with 0.02-0.03% NaHCO3.
Purity
Greater than 99.0% as determined by:
(a) Gel filtration analysis.
(b) Analysis by SDS-PAGE.Biological Activity
Is fully biologically active as evidenced by inducing proliferation of Nb2 cells.More Info
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Introduction
Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.
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Synonyms
Mammotropin, Luteotropic hormone, Luteotropin, PRL.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Prolactin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Prl 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.
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Solubility
It is recommended to reconstitute the lyophilized Prolactin in sterile 18MΩ-cm H2O or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
The sequence of the first six N-terminal amino acids was determined and was found to be Ala-Thr-Pro-Val-Cys-Pro.
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Protein content
Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.93 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC DNAman computer analysis program of protein sequences.
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.
- View Data Sheet
Name :
LL-37Description:
LL-37
LL37, antibacterial protein LL-37, cathelicidin LL 37, camp.
Product # :
HOR-041Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
LL-37 Synthetic is a single, non-glycosylated polypeptide chain containing 37 amino acids, having a molecular mass of 4493 Dalton and a Molecular formula of C205H340N60O53.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
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Synonyms
LL37, antibacterial protein LL-37, cathelicidin LL 37, camp.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized LL-37 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LL-37 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.
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Solubility
It is recommended to reconstitute the lyophilized LL-37 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
H-Leu-Leu-Gly-Asp-Phe-Phe-Arg-Lys-Ser-Lys-Glu-Lys-Ile-Gly-Lys-Glu-Phe-Lys-Arg-Ile-Val-Gln-Arg-Ile-Lys-Asp-Phe-Leu-Arg-Asn-Leu-Val-Pro-Arg-Thr-Glu-Ser-OH.
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Background
LL-37, a prominent member of the human cathelicidin family, has emerged as a pivotal host defense peptide with diverse biological functions. This research paper aims to provide a comprehensive analysis of LL-37, elucidating its biochemical properties, antimicrobial activity, immunomodulatory effects, and potential therapeutic applications.
LL-37, derived from the precursor protein hCAP18, plays a crucial role in innate immunity and host defense against microbial pathogens. Beyond its well-established antimicrobial properties, LL-37 exhibits various immunomodulatory effects, making it an intriguing target for therapeutic interventions (Lai & Gallo, 2009). This paper aims to delve into the complexities of LL-37, uncovering its multifaceted nature and potential clinical applications.
LL-37 is a cationic peptide characterized by a helical structure that facilitates its interaction with microbial membranes. Its amphipathic nature enables it to penetrate microbial membranes, leading to disruption and subsequent cell death (Zaiou, 2007). Additionally, LL-37 can undergo proteolytic processing to release smaller bioactive fragments with distinct functions (Bowdish et al., 2005).
LL-37's antimicrobial activity extends beyond direct microbial killing. It also exhibits immunomodulatory effects, stimulating the recruitment of immune cells and promoting the clearance of pathogens through phagocytosis (Scott et al., 2002). Furthermore, LL-37 can neutralize endotoxins, reducing inflammation caused by microbial products (Davidson et al., 2004).
LL-37 possesses immunomodulatory properties that influence various immune cells, including neutrophils, macrophages, dendritic cells, and lymphocytes (Nagaoka et al., 2001). It can promote the differentiation and maturation of immune cells, modulate cytokine production, and contribute to wound healing and tissue repair (van Harten et al., 2018).
The multifunctional nature of LL-37 renders it a promising candidate for various therapeutic applications. LL-37-based therapies are being explored in wound healing, infectious diseases, and immune-related disorders (Pena et al., 2014). Furthermore, LL-37 has shown potential as a vaccine adjuvant, enhancing the immune response to antigens (Howell et al., 2018).
LL-37's diverse roles in immunity and host defense warrant further research to unravel its precise mechanisms of action and potential applications in clinical medicine. As we deepen our understanding of LL-37's complexities, its therapeutic potential continues to expand, offering exciting prospects for the future.
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.