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Description:

Eukaryotic Translation Elongation Factor 1 Beta 2 Human Recombinant

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

Product # :

PRO-167

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Description

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

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Elongation factor 1-beta (EEF1B2) is a translation elongation factor. EEF1B2 is a guanine nucleotide exchange factor which is involved in the transfer of aminoacylated tRNAs to the ribosome. Both EEF1B2 and EEF1D stimulate the exchange of GDP bound to EEF1A to GTP.
Synonyms
Elongation factor 1-beta, EF-1-beta, EEF1B2, EEF1B, EF1B, EEF1B1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGFGDLKSPA GLQVLNDYLA DKSYIEGYVP SQADVAVFEA VSSPPPADLC HALRWYNHIK SYEKEKASLP GVKKALGKYG PADVEDTTGS GATDSKDDDD IDLFGSDDEE ESEEAKRLRE ERLAQYESKK AKKPALVAKS SILLDVKPWD DETDMAKLEE CVRSIQADGL VWGSSKLVPV GYGIKKLQIQ CVVEDDKVGT DMLEEQITAF EDYVQSMDVA AFNKILEHHH HHH.

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

Description:

Interleukin 11 Receptor Subunit Alpha Rat Recombinant

Interleukin-11 receptor subunit alpha, IL-11 receptor subunit alpha, IL-11R subunit alpha, IL-11R-alpha, IL-11RA, Il11ra1.

Product # :

CYT-990

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Description

Interleukin 11 Receptor Subunit Alpha Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 356 amino acids (24-371a.a.) and having a molecular mass of 39.2kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).IL11RA is fused with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL11RA protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

SDS-PAGE

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Introduction
Interleukin 11 Receptor Subunit Alpha (IL11RA) which belongs to the hematopoietic cytokine receptor family is a receptor for interleukin-11. Interleukin 11 is a stromal cell-derived cytokine which is a member of a family of pleiotropic and redundant cytokines that employ the gp130 transducing subunit in their high affinity receptors. This specific receptor is quite similar to ciliary neurotrophic factor, since both contain an extracellular region with a two-domain structure composed of an immunoglobulin-like domain and a cytokine receptor-like domain. The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 are able to utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex is involved in the control of proliferation and/or differentiation of skeletogenic progenitor or additional mesenchymal cells.
Synonyms
Interleukin-11 receptor subunit alpha, IL-11 receptor subunit alpha, IL-11R subunit alpha, IL-11R-alpha, IL-11RA, Il11ra1.
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
TPCPQAWGPP GVQYGQPGRP VMLCCPGVNA GTPVSWFRDG DSRLLQGPDS GLGHRLVLAQ VDSRDEGTYV CRTLDGVFGG MVTLKLGSPP ARPEVSCQAV DYENFSCTWS PGRVSGLPTR YLTSYRKKTL PGAESQRESP STGPWPCPQD PLEASRCVVH GAEFWSEYRI NVTEVNPLGA STCLLDVRLQ RILRPDPPQG LRVESVPGYP RRLHASWTYP ASWRRQPHFL LKFRLQYRPA QHPAWSTVEP IGLEELITDA VAGLPHAVRV SARDFLDAGT WSAWSPEAWG TPSTGPLRDE VPDGSRGHEQ KLEAAAQEDS PAPPSPSLQP DPRPLDHRDP LEQVAVLAVE HHHHHH.
Background
What is the molecular weight/Mw of IL11RA RAT Protein?
IL11RA RAT Protein has a total Mw of 39.2kDa.

What is the source or expression system of IL11RA RAT Protein?
Sf9, Baculovirus cells.

What is the Purity of IL11RA RAT Protein?
IL11RA RAT Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of IL11RA RAT Protein?
The biological functionality of IL11RA RAT Protein will be determined in the future.

What is the amino acid sequence of IL11RA RAT Protein?
TPCPQAWGPP GVQYGQPGRP VMLCCPGVNA GTPVSWFRDG DSRLLQGPDS GLGHRLVLAQ VDSRDEGTYV CRTLDGVFGG MVTLKLGSPP ARPEVSCQAV DYENFSCTWS PGRVSGLPTR YLTSYRKKTL PGAESQRESP STGPWPCPQD PLEASRCVVH GAEFWSEYRI NVTEVNPLGA STCLLDVRLQ RILRPDPPQG LRVESVPGYP RRLHASWTYP ASWRRQPHFL LKFRLQYRPA QHPAWSTVEP IGLEELITDA VAGLPHAVRV SARDFLDAGT WSAWSPEAWG TPSTGPLRDE VPDGSRGHEQ KLEAAAQEDS PAPPSPSLQP DPRPLDHRDP LEQVAVLAVE HHHHHH.
What applications can IL11RA RAT Protein be used in?
IL11RA RAT Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL11RA RAT Protein?
The endotoxin level is minimal, IL11RA RAT Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL11RA RAT that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL11RA RAT?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

HIV-1 p24 Mouse antibody

Product # :

ANT-152

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Shipped at Room temp

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Formulation

1mg/ml in PBS (after reconstitution).

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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.
Solubility
Reconstitute with H20. Mix gently, wash the sides of the vial and wait 30-60 seconds before use.
Immunogen
r.HIV-1p24.
Ig Subclass
mouse IgG1.
Clone
YDHIV1gp24.
Titer
By direct ELISA (against recombinant gp24), 1:10,000 dilution will yield 0.4 O.D using alkaline phosphatase conjugated rabbit anti-mouse Ig (Jackson Laboratories).
Shipping Conditions
Antibody is shipped lyophilized at ambient temperature.
Type
Mouse antibody Monoclonal.
Storage Procedures
In lyophilized form, for long periods, store at 4C in a dry environment. After reconstitution, if not intended for use within a month, aliquot and store at -20C.
Purification Method
Ion exchange column.

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.

Description:

Chaperone Protein hchA E.Coli Recombinant

Chaperone protein hchA, EcHsp31, Hsp31, hchA, yedU, yzzC, b1967, JW1950.

Product # :

HSP-043

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Description

hchA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 303 amino acids (1-283 a.a.) and having a molecular mass of 33.3kDa.hchA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Escherichia coli Hsp31 (HchA) is a homodimeric member of the ThiI/DJ-1/PfpI superfamily which combines molecular chaperone and aminopeptidase activities. HchA uses temperature-induced exposure of structured hydrophobic domains to capture and stabilize early unfolding protein intermediates under severe thermal stress.
Synonyms
Chaperone protein hchA, EcHsp31, Hsp31, hchA, yedU, yzzC, b1967, JW1950.
Physical Appearance
Sterile filtered colorless solution.
Stability
hchA E.Coli Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTVQTSKNPQ VDIAEDNAFF PSEYSLSQYT SPVSDLDGVD YPKPYRGKHK ILVIAADERY LPTDNGKLFS TGNHPIETLL PLYHLHAAGF EFEVATISGL MTKFEYWAMP HKDEKVMPFF EQHKSLFRNP KKLADVVASL NADSEYAAIF VPGGHGALIG LPESQDVAAA LQWAIKNDRF VISLCHGPAA FLALRHGDNP LNGYSICAFP DAADKQTPEI GYMPGHLTWY FGEELKKMGM NIINDDITGR VHKDRKLLTG DSPFAANALG KLAAQEMLAA YAG.

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.

Description:

Melan-A Human Recombinant

MART-1, MART1, Melanoma antigen recognized by T-cells 1, Antigen LB39-AA, Antigen SK29-AA, Protein Melan-A, MLANA.

Product # :

PRO-1498

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Description

MLANA Human Recombinant produced in E. coli is a single polypeptide chain containing 94 amino acids (48-118) and having a molecular mass of 10.4kDa. MLANA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Melan-A (MLANA), is engaged in melanosome biogenesis by ensuring the stability of GPR143. MLANA takes part in the expression, stability, trafficking, and processing of melanocyte protein PMEL, which is essential to the formation of stage II melanosomes.
Synonyms
MART-1, MART1, Melanoma antigen recognized by T-cells 1, Antigen LB39-AA, Antigen SK29-AA, Protein Melan-A, MLANA.
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 MGSCRRRNGY RALMDKSLHV GTQCALTRRC PQEGFDHRDS KVSLQEKNCE PVVPNAPPAY EKLSAEQSPP PYSP.

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.

Description:

Methylmalonic Aciduria Type B Human Recombinant

CBIB, Cob(I)alamin adenosyltransferase, EC 2.5.1.17.

Product # :

ENZ-248

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Description

MMAB Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 239 amino acids (33-250 a.a.) and having a molecular mass of 26.3 kDa. The MMAB is fused to 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

MMAB 1mg/ml protein solution contains 20mM Tris pH-7.5 & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
MMAB protein catalyzes the last step in the conversion of vitamin B(12) into adenosylcobalamin (AdoCbl), a vitamin B12 containing coenzyme for methylmalonyl-CoA mutase(MCM). Decreased MMAB activity leads to the inherited disorder vitamin B12 dependent methylmalonic aciduria linked to the cblB complementation group.
Synonyms
CBIB, Cob(I)alamin adenosyltransferase, EC 2.5.1.17.
Physical Appearance
Sterile Filtered clear solution.
Stability
MMAB Human although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQSRGPQGVE DGDRPQPSSK TPRIPKIYTK TGDKGFSSTF TGERRPKDDQ VFEAVGTTDE LSSAIGFALE LVTEKGHTFA EELQKIQCTL QDVGSALATP CSSAREAHLK YTTFKAGPIL ELEQWIDKYT SQLPPLTAFI LPSGGKISSA LHFCRAVCRR AERRVVPLVQ MGETDANVAK FLNRLSDYLF TLARYAAMKE GNQEKIYKKN DPSAESEGL.

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.

Description:

Adenosine Deaminase-Like Human Recombinant

Adenosine Deaminase-Like, Adenosine Deaminase-Like Protein, EC 3.5.4.-, EC 3.5.4, ADAL.

Product # :

ENZ-788

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Description

ADAL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 292 amino acids (1-267) and having a molecular mass of 32.7kDa.ADAL is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The ADAL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.4M Urea.

Purity

Greater than 80% as determined by Analysis by SDS-PAGE.

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Introduction
Adenosine deaminase-like protein (ADAL) is a putative nucleoside deaminase. ADAL catalyzes the hydrolytic deamination of adenosine or some similar substrate and has a role in purine metabolism.
Synonyms
Adenosine Deaminase-Like, Adenosine Deaminase-Like Protein, EC 3.5.4.-, EC 3.5.4, ADAL.
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 MGSEFMIEAE EQQPCKTDFY SELPKVELHA HLNGSISSHT MKKLIAQKPD LKIHDQMTVI DKGKKRTLEE CFQMFQTIHQ LTSSPEDILM VTKDVIKEFA DDGVKYLELR STPRRENATG MTKKTYVESI LEGIKQSKQE NLDIDVRYLI AVDRRGGPLV AKETVKLAEE FFLSTEGTVL GLDLSGDPTV GQAKDFLEPL LEAKKAGLKL ALHLSEIPNQ KKETQILLDL LPDRIGHGTF LNSGEGGSLD LVDFVRQHRI PLGKAWSFRS SR.

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.

Description:

E-Selectin Human Recombinant, Sf9

E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E

Product # :

PRO-2712

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Description

SELE Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 541 amino acids (22-556 a.a) and having a molecular mass of 59.4kDa.SELE is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

The SELE solution (0.5mg/1ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Measured by the ability of the immobilized protein to support the adhesion of U937 human histiocytic lymphoma cells, which are added to human E-Seletin/CD62E coated plates 2ug/ml. This effect is > 40%.

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Introduction
E-selectin (SELE) is a part of a family of divalent cation-dependent carbohydrate-binding glycoproteins or adhesion molecules. E-selectin is expressed on the surface of endothelial cells and mediates the interaction of leukocytes and platelets with endothelial cells during an inflammatory response. E-selectin is present in single copy in the human genome and contains 14 exons spanning about 13 kb of DNA.
Synonyms
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E
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
WSYNTSTEAM TYDEASAYCQ QRYTHLVAIQ NKEEIEYLNS ILSYSPSYYW IGIRKVNNVW VWVGTQKPLT EEAKNWAPGE PNNRQKDEDC VEIYIKREKD VGMWNDERCS KKKLALCYTA ACTNTSCSGH GECVETINNY TCKCDPGFSG LKCEQIVNCT ALESPEHGSL VCSHPLGNFS YNSSCSISCD RGYLPSSMET MQCMSSGEWS APIPACNVVE CDAVTNPANG FVECFQNPGS FPWNTTCTFD CEEGFELMGA QSLQCTSSGN WDNEKPTCKA VTCRAVRQPQ NGSVRCSHSP AGEFTFKSSC NFTCEEGFML QGPAQVECTT QGQWTQQIPV CEAFQCTALS NPERGYMNCL PSASGSFRYG SSCEFSCEQG FVLKGSKRLQ CGPTGEWDNE KPTCEAVRCD AVHQPPKGLV RCAHSPIGEF TYKSSCAFSC EEGFELHGST QLECTSQGQW TEEVPSCQVV KCSSLAVPGK INMSCSGEPV FGTVCKFACP EGWTLNGSAA RTCGATGHWS GLLPTCEAPT ESNIPHHHHH 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.

Description:

Major Histocompatibility Complex Class II DO Beta Human Recombinant

HLA class II histocompatibility antigen, DO beta chain, MHC class II antigen DOB, HLA-DOB, Major histocompatibility complex, class II, DO beta, DOB.

Product # :

PRO-1967

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Description

HLA-DOB Human Recombinant produced in E. coli is a single polypeptide chain containing 222 amino acids (27-224) and having a molecular mass of 25.2 kDa.HLA-DOB is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

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

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Major Histocompatibility Complex Class II DO Beta (HLA-DOB) is a part of the HLA class II beta chain paralogues. This class II beta chain is a heterodimer which is located in intracellular vesicles and consists of an alpha (DOA) and a beta chain (DOB), both anchored in the membrane. HLA-DOB which interacts with the HLA-DM molecule in B-cells is a significant modulator in the HLA class II restricted antigen presentation pathway. Class II molecules are expressed in antigen presenting cells such as B lymphocytes, dendritic cells and macrophages.
Synonyms
HLA class II histocompatibility antigen, DO beta chain, MHC class II antigen DOB, HLA-DOB, Major histocompatibility complex, class II, DO beta, DOB.
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 MGSGTDSPED FVIQAKADCY FTNGTEKVQF VVRFIFNLEE YVRFDSDVGM FVALTKLGQP DAEQWNSRLD LLERSRQAVD GVCRHNYRLG APFTVGRKVQ PEVTVYPERT PLLHQHNLLH CSVTGFYPGD IKIKWFLNGQ EERAGVMSTG PIRNGDWTFQ TVVMLEMTPE LGHVYTCLVD HSSLLSPVSV EWRAQSEYSW RK.

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.

Description:

Nucleoside Diphosphate Kinase E.Coli Recombinant

Nucleoside diphosphate kinase, NDK, NDP kinase, Nucleoside-2-P kinase, b2518, JW2502.

Product # :

PKA-034

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Description

NDK E.Coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-143 a.a.) and having a molecular mass of 18kDa.NDK is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

NDK protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.1M NaCl and 1mM DTT.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Nucleoside diphosphate kinase (Ndk) is an enzyme which catalyzes the exchange of phosphate groups between different nucleoside diphosphates. Ndk’s activity sustains equilibrium between the concentrations of various nucleoside triphosphates for example, when GTP is produced in the citric acid (Krebs) cycle is converted to ATP. Ndk has a key role in the synthesis of nucleoside triphosphates other than ATP.
Synonyms
Nucleoside diphosphate kinase, NDK, NDP kinase, Nucleoside-2-P kinase, b2518, JW2502.
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 MGSHMAIERT FSIIKPNAVA KNVIGNIFAR FEAAGFKIVG TKMLHLTVEQ ARGFYAEHDG KPFFDGLVEF MTSGPIVVSV LEGENAVQRH RDLLGATNPA NALAGTLRAD YADSLTENGT HGSDSVESAA REIAYFFGEG EVCPRTR.

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.

Description:

NECAP Endocytosis Associated 2 Human Recombinant

NECAP endocytosis-associated protein 2, NECAP-2, FLJ10420, Adaptin ear-binding coat-associated protein 2.

Product # :

PRO-180

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Description

NECAP2 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 283 amino acids (1-263a.a.) and having a molecular mass of 30.5 kDa. NECAP2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The NECAP2 protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 2mM DTT and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
NECAP2 which is involved in endocytosis, is a vital protein paralogues for clathrin-mediated membrane trafficking which are enhanced in CCV layers. NECAP2 protein colocalizes with AP-2 at the plasma membrane by binding AP-2s ?-ear domain, and interacts with AP-1, AP-2 and several GAE domain proteins termed GGA1, GGA2 and GGA3.
Synonyms
NECAP endocytosis-associated protein 2, NECAP-2, FLJ10420, Adaptin ear-binding coat-associated protein 2.
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 MEESGYESVL CVKPDVHVYR IPPRATNRGY RAAEWQLDQP SWSGRLRITA KGQMAYIKLE DRTSGELFAQ APVDQFPGTA VESVTDSSRY FVIRIEDGNG RRAFIGIGFG DRGDAFDFNV ALQDHFKWVK QQCEFAKQAQ NPDQGPKLDL GFKEGQTIKL NIANMKKKEG AAGNPRVRPA STGGLSLLPP PPGGKTSTLI PPPGEQLAVG GSLVQPAVAP SSGGAPVPWP QPNPATADIW GDFTKSTGST SSQTQPGTGW VQF

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.

Description:

BCL2/Adenovirus E1B 19kDa Interacting Protein 1 Human Recombinant

BCL2/Adenovirus E1B 19kDa Interacting Protein 1, NIP1, BCL2/Adenovirus E1B 19 KDa Protein-Interacting Protein 1, Transformation-Related Gene 8 Protein, TRG-8, BCL2/Adenovirus E1B 19kD-Interacting Protein 1, Vesicle Transport Protein SEC20, SEC20L, SEC20, Vesicle transport protein SEC20.

Product # :

PRO-2150

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Description

BNIP1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (1-199 a.a) and having a molecular mass of 25.2kDa. BNIP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

BNIP1 protein solution (1.0 mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
BNIP1 belongs to the of the BCL2/adenovirus E1B 19 kd-interacting protein (BNIP) family. BNIP1 interacts with the E1B 19 kDa protein, which defends cells from virally-induced cell death. In addition, BNIP1 interacts with E1B 19 kDa-like sequences of BCL2 which is an additional apoptotic protector. Adding up, BNIP1 is implicated in vesicle transport into the endoplasmic reticulum. Alternative splicing results of BNIP1 in four protein products with identical N- and C-termini have been found.
Synonyms
BCL2/Adenovirus E1B 19kDa Interacting Protein 1, NIP1, BCL2/Adenovirus E1B 19 KDa Protein-Interacting Protein 1, Transformation-Related Gene 8 Protein, TRG-8, BCL2/Adenovirus E1B 19kD-Interacting Protein 1, Vesicle Transport Protein SEC20, SEC20L, SEC20, Vesicle transport protein SEC20.
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 MGSMAAPQDV HVRICNQEIV KFDLEVKALI QDIRDCSGPL SALTELNTKV KEKFQQLRHR IQDLEQLAKE QDKESEKQLL LQEVENHKKQ MLSNQASWRK ANLTCKIAID NLEKAELLQG GDLLRQRKTT KESLAQTSST ITESLMGISR MMAQQVQQSE EAMQSLVTSS RTILDANEEF KSMSGTIQLG RKLITKYNRR EL.

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.

Description:

Exodus-2 Mouse Recombinant (CCL21)

Small inducible cytokine A21, CCL21, Beta chemokine exodus-2, 6Ckine, Secondary lymphoid-tissue chemokine, SLC, chemokine (C-C motif) ligand 21, ECL, CKb9, TCA4, SCYA21, MGC34555.

Product # :

CHM-371

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Description

Exodus-2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 110 amino acids and having a molecular mass of 12kDa. The CCL21 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM Phosphate buffer and 0.15M NaCl pH-7.4.

Purity

Greater than 97.0% as determined by SDS-PAGE & RP-HPLC.

Biological Activity

Determined by its ability to chemoattract total murine T cell population using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

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Introduction
Chemokine (C-C motif) ligand 21 (CCL21) is a small cytokine belonging to the CC chemokine family. This chemokine is also known as 6Ckine (because it has six conserved cysteine residues instead of the four cysteines typical to chemokines), exodus-2, and secondary lymphoid-tissue chemokine (SLC). CCL21 is expressed predominantly in the lymph nodes and, in contrast to other CC chemokines, is chemotactic for lymphocytes. The gene for CCL21 is located on human chromosome 9. CCL21 elicits its effects by binding to a cell surface chemokine receptor known as CCR7.
Synonyms
Small inducible cytokine A21, CCL21, Beta chemokine exodus-2, 6Ckine, Secondary lymphoid-tissue chemokine, SLC, chemokine (C-C motif) ligand 21, ECL, CKb9, TCA4, SCYA21, MGC34555.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Exodus-2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL21 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 Exodus2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions
Amino Acid Sequence
SDGGGQDCCL KYSQKKIPYS IVRGYRKQEP SLGCPIPAIL FLPRKHSKPE LCANPEEGWV QNLMRRLDQP PAPGKQSPGC RKNRGTSKSG KKGKGSKGCK RTEQTQPSRG.
Background
What is the molecular weight/Mw of CCL21 MOUSE Protein?
CCL21 MOUSE Protein has a total Mw of 12kDa.

What is the source or expression system of CCL21 MOUSE Protein?
Escherichia Coli.

What is the Purity of CCL21 MOUSE Protein?
CCL21 MOUSE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CCL21 MOUSE Protein?
Determined by its ability to chemoattract total murine T cell population using a concentration range of 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.

What is the amino acid sequence of CCL21 MOUSE Protein?
SDGGGQDCCL KYSQKKIPYS IVRGYRKQEP SLGCPIPAIL FLPRKHSKPE LCANPEEGWV QNLMRRLDQP PAPGKQSPGC RKNRGTSKSG KKGKGSKGCK RTEQTQPSRG.

What applications can CCL21 MOUSE Protein be used in?
CCL21 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CCL21 MOUSE Protein?
The endotoxin level is minimal, CCL21 MOUSE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CCL21 MOUSE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CCL21 MOUSE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Interleukin-8 Rhesus Macaque Recombinant

IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP

Product # :

CHM-004

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Description

IL 8 Rhesus Macaque Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 79 amino acids and having a molecular mass of 9.1kDa.The IL 8 Rhesus Macaque is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

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

Purity

Greater than 97.0% as determined by SDS-PAGE.

Biological Activity

Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 50-150ng/ml, corresponding to a Specific Activity of 6,667-20,000IU/mg.

More Info

Introduction
Interleukin-8 (IL-8) is a chemokine produced by macrophages and other cell types such as epithelial cells. It is also synthesized by endothelial cells, which store IL-8 in their storage vesicles, the Weibel-Palade bodies.When first encountering an antigen, the primary cells to encounter it are the macrophages who phagocytose the particle. Upon processing, they release chemokines to signal other immune cells to come in to the site of inflammation. IL-8 is one such chemokine. It serves as a chemical signal that attracts neutrophils at the site of inflammation, and therefore is also known as Neutrophil Chemotactic Factor.
Synonyms
IL-8, CXCL8, Monocyte-derived neutrophil chemotactic factor, MDNCF, T-cell chemotactic factor, Neutrophil-activating protein 1, NAP-1, Protein 3-10C, Granulocyte chemotactic protein 1, GCP-1, Monocyte-derived neutrophil-activating peptide, MONAP, Emoctakin, K60, NAF, LECT, LUCT, 3-10C, LYNAP, SCYB8, TSG-1, AMCF-I, b-ENAP
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized IL-8 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL-8 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized IL-8 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AVLPRSAKEL RCECIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE PWVQRVVEKF VKRAENQNP
Background
What is the molecular weight/Mw of CXCL8 MACAQUE Protein?
CXCL8 MACAQUE Protein has a total Mw of 9.1kDa.

What is the source or expression system of CXCL8 MACAQUE Protein?
Escherichia Coli.

What is the Purity of CXCL8 MACAQUE Protein?
CXCL8 MACAQUE Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL8 MACAQUE Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 50-150ng/ml, corresponding to a Specific Activity of 6,667-20,000IU/mg.

What is the amino acid sequence of CXCL8 MACAQUE Protein?
AVLPRSAKEL RCECIKTYSK PFHPKFIKEL RVIESGPHCA NTEIIVKLSD GRELCLDPKE PWVQRVVEKF VKRAENQNP

What applications can CXCL8 MACAQUE Protein be used in?
CXCL8 MACAQUE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL8 MACAQUE Protein?
The endotoxin level is minimal, CXCL8 MACAQUE Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL8 MACAQUE that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL8 MACAQUE?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

GRO-Alpha Human Recombinant (CXCL1)

Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.

Product # :

CHM-329

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Description

GRO Alpha Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 73 amino acids and having a molecular mass of 7811 Dalton. The GRO-alpha is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in 20mM PB, pH 7.4, 50mM NaCl.

Purity

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

Biological Activity

Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

sds-page

More Info

Introduction
Chemokine (C-X-C motif) ligand 1 (CXCL1) is a small cytokine belonging to the CXC chemokine family that was previously called GRO1 oncogene, Neutrophil-activating protein 3 (NAP-3) and melanoma growth stimulating activity, alpha (MSGA-a). It is secreted by human melanoma cells, has mitogenic properties and is implicated in melanoma pathogenesis. CXCL1 is expressed by macrophages, neutrophilsand epithelial cells, and has neutrophil chemoattractant activity. CXCL1 plays a role in spinal cord development by inhibiting the migration of oligodendrocyte precursors and is involved in the processes of angiogenesis, inflammation, wound healing, and tumorigenesis. This chemokine elicits its effects by signaling through the chemokine receptor CXCR2. The gene for CXCL1 is located on human chromosome 4 amongst genes for other CXC chemokines.
Synonyms
Growth-regulated protein alpha, CXCL1, Melanoma growth stimulatory activity, MGSA, Neutrophil-activating protein 3, NAP-3, GRO-alpha (1-73), chemokine (C-X-C motif) ligand 1, GRO1, GROa, SCYB1, MGSA-a, MGSA alpha.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GRO-alpha although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL1 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 CXCL1 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.
Background
What is the molecular weight/Mw of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein has a total Mw of 7.81kDa.

What is the source or expression system of CXCL1 HUMAN Protein?
Escherichia Coli.

What is the Purity of CXCL1 HUMAN Protein?
CXCL1 HUMAN Protein is >97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL1 HUMAN Protein?
Determined by its ability to chemoattract human peripheral blood neutrophils using a concentration range of 10.0-100.0 ng/ml.

What is the amino acid sequence of CXCL1 HUMAN Protein?
The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Ser-Val-Ala-Thr.

What applications can CXCL1 HUMAN Protein be used in?
CXCL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL1 HUMAN Protein?
The endotoxin level is minimal, CXCL1 HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant CXCL1 HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of CXCL1 HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Vascular cell adhesion molecule 1 Human Recombinant, HEK

Vascular cell adhesion protein 1, V-CAM 1, INCAM-100, CD106, VCAM1, L1CAM, MGC99561, DKFZp779G2333.

Product # :

PRO-1641

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Description

VCAM1 Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 682 amino acids (25-698). VCAM1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

VCAM1 was lyophilized from a 0.2 µM filtered solution of 20mM PB, 150mM NaCl, 2mM CaCl2, 2mM MgCl2 and 5%Threhalose, pH 7.2.

Purity

Greater than 95% as determined by SDS-PAGE.

More Info

Introduction
VCAM1 is a member of the Ig superfamily. It is a cell surface sialoglycoprotein expressed by cytokine activated endothelium. VCAM-1 contains 6 or 7 immunoglobulin domains, and is expressed on both large and small vessels only after the endothelial cells are stimulated by cytokines. The protein has a number of functions including the regulation of leukocyte migration, leukocyte endothelial cell adhesion and signal transduction and may play a role in a number of inflammatory diseases (artherosclerosis and rheumatoid arthritis).
Synonyms
Vascular cell adhesion protein 1, V-CAM 1, INCAM-100, CD106, VCAM1, L1CAM, MGC99561, DKFZp779G2333.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized VCAM1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution VCAM1 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized VCAM1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
FKIETTPESRYLAQIGDSVSLTCSTTGCESPFFSWRTQIDSPLNGKVTNEGTTS
TLTMNPVSFGNEHSYLCTATCESRKLEKGIQVEIYSFPKDPEIHLSGPLEAGKP
ITVKCSVADVYPFDRLEIDLLKGDHLMKSQEFLEDADRKSLETKSLEVTFTPVIE
DIGKVLVCRAKLHIDEMDSVPTVRQAVKELQVYISPKNTVISVNPSTKLQEGGSVT
MTCSSEGLPAPEIFWSKKLDNGNLQHLSGNATLTLIAMRMEDSGIYVCEGVNLIGKNRKEV
ELIVQEKPFTVEISPGPRIAAQIGDSVMLTCSVMGCESPSFSWRTQIDSPLSGKVRSEGTN
STLTLSPVSFENEHSYLCTVTCGHKKLEKGIQVELYSFPRDPEIEMSGGLVNGSSVTVSCKV
PSVYPLDRLEIELLKGETILENIEFLEDTDMKSLENKSLEMTFIPTIEDTGKALVCQAKLHID
DMEFEPKQRQSTQTLYVNVAPRDTTVLVSPSSILEEGSSVNMTCLSQGFPAPKILWSRQLPNGE
LQPLSENATLTLISTKMEDSGVYLCEGINQIRKAQLKDAGVYECESKNKVGSQLRSLTLDVQGRE
NNKDYFSPEVDHHHHHHAGRSRKEVELIIQVTPKDIKLTAFPSESVKEGDTVIISCTCGNVPETW
IILKKKAETGDTVLKSIDGAYTIRKAQLKDAGVYECESKNKVGSQLRSLTLDVQGRENNKDYFSPE
VDHHHHHH.

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.

Description:

Recombinant Human Anti HER2

Product # :

ANT-602

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Description

Recombinant Human Anti HER2 is produced by recombinant DNA technology in a Chinese Hamster Ovary mammalian cell expression system in a serum-free medium and has a molecular weight of approximately 148 kDa.

Source

CHO.

Formulation

Each ml of Recombinant HER2 Antibody solution (32.1mg/ml) contains 0.56mg histidine-HCl, 0.36mg histidine and 0.1mg polysorbate-20, pH-6.

Purity

Should be not less than 95.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The ED₅₀ as determined by the proliferation inhibition of BT474 cell, Perform a comparison of a dilution series of the Sample solution with a dilution series of the Standard solution, measured potency was found to be 0.9 x 10⁴EU/mg.

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Introduction
HER-2/neu (erbB-2) encodes an 185-kDa orphan receptor tyrosine kinase that is constitutively active as a dimer and displays potent oncogenic activity when overexpressed. Herstatin, as the product of alternative HER-2 transcript, retains intron 8. The herstatin mRNA is expressed in normal human fetal kidney and liver, but is at reduced levels relative to p185HER-2 mRNA in carcinoma cells that contain an amplified HER-2 gene. Herstatin appears to be an inhibitor of p185HER-2, because it disrupts dimers, reduces tyrosine phosphorylation of p185, and inhibits the anchorage-independent growth of transformed cells that overexpress HER-2.
Physical Appearance
Sterile filtered colorless liquid formulation.
Stability
Recombinant Human Anti HER2 should be stored between 2-8°C.
Amino Acid Sequence
LIGHT CHAIN
DIQMTQSPSSLSASVGDRVTITCRASQDVNTAVAWYQQ
KPGKAPKLLIYSASFLYSGVPSRFSGSRSGTDFTLTISSL
QPEDFATYYCQQHYTTPPTFGQGTKVEIKRTVAAPSVFI
FPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQ
SGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYAC
EVTHQGLSSPVTKSFNRGEC.

HEAVY CHAIN
EVQLVESGGGLVQPGGSLRLSCAASGFNIKDTYIHWVR
QAPGKGLEWVARIYPTNGYTRYADSVKGRFTISADTSK
NTAYLQMNSLRAEDTAVYYCSRWGGDGFYAMDYWGQ
GTLVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKD
YFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVT
VPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHTCP
PCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVS
HEDPEVKFNWYVDGVEVHNAKTKPREEQYNSTYRVVSV
LTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPR
EPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWE
SNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQ
GNVFSCSVMHEALHNHYTQKSLSLSPGK.

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.

Description:

Epidermal Growth Factor Mouse Recombinant, His Tag

Urogastrone, URG, EGF.

Product # :

CYT-138

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Description

EGF mouse Recombinant produced in E. coli is a single polypeptide chain containing 77 amino acids (977-1029) and having a molecular mass of 8.6kDa.EGF is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The EGF solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 2mM DTT and 10% glycerol.

Purity

Greater than 90% as determined by SDS-PAGE.

SDS-PAGE

More Info

Introduction
Epidermal growth factor has a profound effect on the differentiation of specific cells in vivo and is a potent mitogenic factor for a variety of cultured cells of both ectodermal and mesodermal origin. The EGF precursor is believed to exist as a membrane-bound molecule which is proteolytically cleaved to generate the 53-amino acid peptide hormone that stimulates cells to divide.
EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture.
Synonyms
Urogastrone, URG, EGF.
Physical Appearance
Sterile Filtered 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 MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.
Background
Unveiling Epidermal Growth Factor Mouse Recombinant: Harnessing His Tag for Enhanced Insights and Therapeutic Prospects
Abstract:
This research paper delves into the realm of Epidermal Growth Factor Mouse Recombinant (EGF-MR), focusing on the strategic integration of a Histidine (His) Tag. By employing sophisticated methodologies encompassing protein engineering, chromatographic techniques, and cellular assays, this study unveils the multifaceted molecular attributes of EGF-MR with His Tag. The findings not only enhance our understanding of EGF-MR's behavior but also illuminate potential avenues for therapeutic interventions.
Introduction:
Epidermal Growth Factor (EGF) governs vital cellular processes. This paper delves into Epidermal Growth Factor Mouse Recombinant (EGF-MR) with a specific emphasis on the incorporation of a Histidine (His) Tag, unraveling its molecular intricacies and therapeutic implications.
Protein Engineering and His Tag Integration:
The paper navigates the tailored engineering of EGF-MR to accommodate a His Tag, a peptide sequence that facilitates protein purification. The process involves strategic modification of the EGF-MR gene to ensure proper folding and presentation of the His Tag.
Chromatographic Purification and His Tag Affinity:
Chromatographic techniques, specifically immobilized metal ion affinity chromatography (IMAC), are employed to purify the His-tagged EGF-MR. The His Tag's high affinity for metal ions facilitates efficient purification, yielding a highly purified and bioactive protein product.
Structural and Functional Insights:
The presence of the His Tag is not just for purification; it serves as a molecular handle to investigate EGF-MR's structural dynamics. High-resolution structural analyses coupled with biophysical assays unravel how the His Tag affects EGF-MR's conformation and binding interactions.
Cellular Assays and Bioactivity Assessment:
In vitro cellular assays, including proliferation and migration studies, provide insights into the impact of His Tag on EGF-MR's bioactivity. Comparative analyses shed light on the functionality of His-tagged EGF-MR and its potential implications in cellular responses.
Therapeutic Prospects and Targeted Delivery:
The incorporation of a His Tag presents a unique avenue for tailored drug delivery. The His Tag can serve as a docking site for targeted therapies, enabling precise interactions with specific receptors on target cells.
Future Directions and Challenges:
While promising, challenges such as potential steric hindrance from the His Tag require consideration. Future research should focus on optimizing the positioning of the His Tag to maintain EGF-MR's full biological activity.
Conclusion:
In a harmonious synthesis of advanced methodologies and innovative insights, the integration of His Tag into Epidermal Growth Factor Mouse Recombinant emerges as a transformative paradigm. The His Tag not only facilitates purification but also offers a molecular window into EGF-MR's behavior, potentially redefining targeted therapies and precision medicine.
What is the molecular weight/Mw of EGF MOUSE, HIS Protein?
EGF MOUSE, HIS Protein has a total Mw of 8.6kDa.

What is the source or expression system of EGF MOUSE, HIS Protein?
Escherichia Coli.

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

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

What is the amino acid sequence of EGF MOUSE, HIS Protein?
MGSSHHHHHH SSGLVPRGSH MGSMNSYPGC PSSYDGYCLN GGVCMHIESL DSYTCNCVIG YSGDRCQTRD LRWWELR.

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

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

Description:

Interleukin-3 Receptor Subunit Alpha Human Recombinant

Interleukin 3 Receptor Subunit Alpha, Interleukin 3 Receptor, Alpha (Low Affinity), IL-3 Receptor Subunit Alpha, IL-3R Subunit Alpha, CD123 Antigen, IL-3R-Alpha, IL-3RA, IL3R, Interleukin-3 Receptor Subunit Alpha, IL-3 Receptor Alpha SP2 Isoform, HIL-3Ra, IL3RAY, CD123, IL3RX, IL3RY, IL3RA.

Product # :

CYT-1049

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Description

IL3RA produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (20-305 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 295 amino acids and having a molecular mass of 34.1kDa.IL3RA is purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL3RA protein solution (0.25mg/ml) contains 10% glycerol & Phosphate buffered saline (pH7.4).

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
IL3RA, also known as Interleukin 3 Receptor Subunit Alpha, is a single-pass type 1 membrane protein which is a member of the type 1 cytokine receptor family as well as type 5 subfamily. IL3RA is a pleiotropic cytokine which is produced mainly by activated T cells or mast cells. Moreover, the specific alpha subunit of the interleukin 3 receptor is strongly expressed in a variety of leukemic blasts as well as leukemic stem cells and appears to be a great target for the therapy of leukemias.
Synonyms
Interleukin 3 Receptor Subunit Alpha, Interleukin 3 Receptor, Alpha (Low Affinity), IL-3 Receptor Subunit Alpha, IL-3R Subunit Alpha, CD123 Antigen, IL-3R-Alpha, IL-3RA, IL3R, Interleukin-3 Receptor Subunit Alpha, IL-3 Receptor Alpha SP2 Isoform, HIL-3Ra, IL3RAY, CD123, IL3RX, IL3RY, IL3RA.
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
ADLKEDPNPP ITNLRMKAKA QQLTWDLNRN VTDIECVKDA DYSMPAVNNS YCQFGAISLC EVTNYTVRVA NPPFSTWILF PENSGKPWAG AENLTCWIHD VDFLSCSWAV GPGAPADVQY DLYLNVANRR QQYECLHYKT DAQGTRIGCR FDDISRLSSG SQSSHILVRG RSAAFGIPCT
DKFVVFSQIE ILTPPNMTAK CNKTHSFMHW KMRSHFNRKF RYELQIQKRM QPVITEQVRD RTSFQLLNPG TYTVQIRARE RVYEFLSAWS TPQRFECDQE EGANTRAWRH HHHHH.
Background
What is the molecular weight/Mw of IL 3 RA HUMAN Protein?
IL 3 RA HUMAN Protein has a total Mw of 34.1kDa.

What is the source or expression system of IL 3 RA HUMAN Protein?
Sf9, Baculovirus cells.

What is the Purity of IL 3 RA HUMAN Protein?
IL 3 RA HUMAN Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of IL 3 RA HUMAN Protein?
The biological functionality of IL 3 RA HUMAN Protein will be determined in the future.

What is the amino acid sequence of IL 3 RA HUMAN Protein?
ADLKEDPNPP ITNLRMKAKA QQLTWDLNRN VTDIECVKDA DYSMPAVNNS YCQFGAISLC EVTNYTVRVA NPPFSTWILF PENSGKPWAG AENLTCWIHD VDFLSCSWAV GPGAPADVQY DLYLNVANRR QQYECLHYKT DAQGTRIGCR FDDISRLSSG SQSSHILVRG RSAAFGIPCT
DKFVVFSQIE ILTPPNMTAK CNKTHSFMHW KMRSHFNRKF RYELQIQKRM QPVITEQVRD RTSFQLLNPG TYTVQIRARE RVYEFLSAWS TPQRFECDQE EGANTRAWRH HHHHH.

What applications can IL 3 RA HUMAN Protein be used in?
IL 3 RA HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL 3 RA HUMAN Protein?
The endotoxin level is minimal, IL 3 RA HUMAN Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL 3 RA HUMAN that is in stock and available to order?
ProSpec has the protein in stock and available for immediate delivery.

Where can I order bulk mg quantities of IL 3 RA HUMAN?
ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

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

Description:

Inhibin-Beta C Chain Human Recombinant

Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.

Product # :

HOR-010

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INHBC Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (237-352) and having a molecular mass of 14.9kDa.INHBC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

The INHBC solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
INHBC, the beta C chain of inhibin, belongs to the TGF-beta superfamily. INHBC formulates heterodimers with beta A and beta B subunits. Other members of the TGF-beta superfamily are Actv's and Inhibins, hormones with contradictory roles which take part in pituitary, hypothalamic, and gonadal hormone secretion, as well as differentiation and growth of numerous cell types.
Synonyms
Inhibin Beta C, Actv Beta-C Chain, IHBC, Inhibin Beta C Chain.
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 MGSGIDCQGG SRMCCRQEFF VDFREIGWHD WIIQPEGYAM NFCIGQCPLH IAGMPGIAAS FHTAVLNLLK ANTAAGTTGG GSCCVPTARR PLSLLYYDRD SNIVKTDIPD MVVEACGCS

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.

Description:

Brain-Derived Neurotrophic Factor Human Recombinant

Brain-Derived Neurotrophic Factor, BDNF, MGC34632.

Product # :

CYT-207

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Description

BDNF Human Recombinant produced in E.Coli is a homodimer, non-glycosylated, polypeptide chain containing 2 x 119 amino acids (and an N-terminal Met) and having a total molecular mass of 28kDa. BDNF Human Recombinant is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The protein was lyophilized with 20mM PB and 400mM NaCl, pH 7.2.

Purity

BDNF is greater than 950% as determined SDS-PAGE.

Biological Activity

The activity was determined using Immobilized Human TrkB-His tag protein 2ug/ml (100 μl/well) for its binding to NHS-Biotin BDNF. The ED50 of was found to be ≤20ng/mL

Activity

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Introduction
BDNF promotes the survival of neuronal populations that are all located either in the central nervous system or directly connected to it. BDNF is a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the cns. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (ltp), long-term depression (ltd), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.
Synonyms
Brain-Derived Neurotrophic Factor, BDNF, MGC34632.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized BDNF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BDNF 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 BDNF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
HSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.
Background
Final Thoughts
Although more research is needed on the safety and effectiveness of BDNF human recombinant, trials suggest that this laboratory-produced protein may be effective in managing and treating several neurological and psychiatric disorders. It's important for experts to stay up to date on the latest developments and research to learn more about potential risks and benefits.
What is the molecular weight/Mw of BDNF Protein?
BDNF Protein has a total Mw of 27kDa.

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

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

What is the Biological Activity of BDNF Protein?
The ED50, as determined by the dose-dependent induction of C6 cells proliferation, is 1.3-2µg/ml.

What is the amino acid sequence of BDNF Protein?
MHSDPARRGE LSVCDSISEW VTAADKKTAV DMSGGTVTVL EKVPVSKGQL KQYFYETKCN PMGYTKEGCR GIDKRHWNSQ CRTTQSYVRA LTMDSKKRIG WRFIRIDTSC VCTLTIKRGR.

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

What is the endotoxin level for BDNF Protein?
The endotoxin level is minimal, BDNF Protein was purified using conventional chromatography techniques.
Protein content
BDNF quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 1.6 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Brain-derived Neurotrophic Factor 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.

Description:

Endoglin Human Recombinant, Sf9

CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.

Product # :

CYT-389

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Description

CD105 Human Recombinant extracellular domain produced in baculovirus is a homodimeric, glycosylated, Polypeptide containing 586 amino acids and having a molecular mass of 61 kDa but as a result of glycosylation, migrates at 90 kDa under reducing conditions in SDS-PAGE. The CD105 is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.

Source

Sf9 Insect Cells.

Formulation

Endoglin was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS.

Purity

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

Biological Activity

Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.

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Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.
The protein consists of a homodimer of 180 kDA with disulfide links. It has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Endoglin has been found to be part of the TGF-beta1 receptor complex. It thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.
Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized Endoglin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD105 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 CD-105 in sterile PBS not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.
Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 90kDa.

What is the source or expression system of CD105 Protein?
Sf9 Insect Cells.

What is the Purity of CD105 Protein?
CD105 Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of CD105 Protein?
Measured by its ability to bind with rhTGF-beta RII/Fc in a functional ELISA. Optimal dilutions should be determined by each laboratory for each application.

What is the amino acid sequence of CD105 Protein?
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTY TTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVL SVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPI TSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLE GVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLID ANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPL ASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKE LVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNI LSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSE FLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPI PKTGTLSCTVALRPKTGS.

What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 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.

Description:

CD100 Human Recombinant HEK

Thesemaphorin family containing 1 Ig-like C2-type domain, 1 PSI domain and 1 Sema domai,Semaphorin-4D, A8, BB18, GR3, SEMA4D, C9orf164, CD100, SEMAJ.

Product # :

PRO-1640

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Description

CD100 Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 721 amino acids (22-734). CD100 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

HEK293 cells.

Formulation

CD100 was lyophilized from a 0.2 µM filtered solution of 20mM PB and 150mM NaCl, PH 7.4.

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Semaphorin-4D (CD100) is a member of the semaphorin family containing 1 Ig-like C2-type domain, 1 PSI domain and 1 Sema domain. CD100 is the cell surface receptor forPLXN1B and PLXNB2 which plays a central role in cell-cell signaling. CD100 stimulates the migration of cerebellar granule cells and of endothelial cells, regulates dendrite and axon branching and morphogenesis. In addition, CD100 has a role in the immune system; it promotes signaling via SRC and PTK2B/PYK2, which subsequently mediates activation of phosphatidylinositol 3-kinase and of the AKT1 signaling cascade.
Synonyms
Thesemaphorin family containing 1 Ig-like C2-type domain, 1 PSI domain and 1 Sema domai,Semaphorin-4D, A8, BB18, GR3, SEMA4D, C9orf164, CD100, SEMAJ.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized CD100 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CD100 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
Solubility
It is recommended to reconstitute the lyophilized CCD100 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MAFAPIPRITWEHREVHLVQFHEPDIYNYSALLLSEDKDTLYIGAREAVFAVNALNISEKQHE
VYWKVSEDKKAKCAEKGKSKQTECLNYIRVLQPLSATSLYVCGTNAFQPACDHLNLTSFKFLG
KNEDGKGRCPFDPAHSYTSVMVDGELYSGTSYNFLGSEPIISRNSSHSPLRTEYAIPWLNEPSF
VFADVIRKSPDSPDGEDDRVYFFFTEVSVEYEFVFRVLIPRIARVCKGDQGGLRTLQKKWTSFL
KARLICSRPDSGLVFNVLRDVFVLRSPGLKVPVFYALFTPQLNNVGLSAVCAYNLSTAEEVFSH
GKYMQSTTVEQSHTKWVRYNGPVPKPRPGACIDSEARAANYTSSLNLPDKTLQFVKDHPLMDDSV
TPIDNRPRLIKKDVNYTQIVVDRTQALDGTVYDVMFVSTDRGALHKAISLEHAVHIIEETQLFQD
FEPVQTLLLSSKKGNRFVYAGSNSGVVQAPLAFCGKHGTCEDCVLARDPYCAWSPPTATCVALHQ
TESPSRGLIQEMSGDASVCPDKSKGSYRQHFFKHGGTAELKCSQKSNSEKTMYLKSSDNRVDHHHHHH.

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.

Description:

Complement C3b Inactivated Mouse

Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.

Product # :

PRO-2813

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Description

Mouse Complement C3b Inactivated produced in Mouse serum having a molecular weight of 175kDa.

Source

Mouse serum.

Formulation

C3b Mouse Inactivated solution contains PBS.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Synonyms
Complement C3, C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1, C3, CPAMD1.
Physical Appearance
Sterile Filtered solution.
Stability
C3b Mouse Inactivated is stable at 4°C if entire vial will be used within 2-4 weeks. Store, frozen below -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.
Background
Complement component 3b (C3b) is a key protein in the complement system, a crucial component of the innate immune response. C3b plays a pivotal role in opsonization, inflammation, and clearance of pathogens and damaged cells. In mouse models, research on C3b has provided valuable insights into its mechanism of action, activity, and implications in immune function. This paper aims to delve into the dynamics of mouse C3b, shedding light on its functional attributes and potential applications in immunological research. C3b Inactivated protein has lost its biological capabilities due to structural changes compared to C3b that has binding sites to factor P, factor H, factor B, factorC5, and factor-I and therefore it destroys these sites.
Significantly, C3b inactivated protein cannot bind factor B and is therefore it cannot participate in complement activation.
C3b inactivated protein still binds tC50 properdin and CR3 receptor.

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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