Search: 1000 results found for "beta 2 microglobulin"

Description:

Human GLP-2

GLP2, GLP-2, GLP 2.

Product # :

HOR-305

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Description

GLP-2 contains 34 amino acids having a molecular mass of 3922.35 Dalton.

Formulation

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

Purity

Greater than 98.0% as determined by RP-HPLC.

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Introduction
GLP-2 functions as an intestinal growth factor, which stimulates intestinal epithelial growth. GLP2 is involved in diabetes-associated bowel growth. GLP2 enhances cell differentiation, playing a role as a cytokine and in tissue regeneration, and mediating cytoprotection. GLP2 is invloded numerous therapeutic applications. GLP2 regulates signaling pathways coupled to cell proliferation and cell death by apoptosis.
GLP-2 is produced by specific post-translational proteolytic cleavage of proGLP. GLP-2 is manufactured by the intestinal endocrine L cell and by several neurons in the central nervous system.
Synonyms
GLP2, GLP-2, GLP 2, Glucagon Like Peptide-2.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized GLP2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution GLP2 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 GLP-2 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
His-Ala-Asp-Gly-Ser-Phe-Ser-Asp-Glu-Met-Asn-Thr-Ile-Leu-Asp-Asn-Leu-Ala-Ala-Arg-Asp-Phe-Ile-Asn-Trp-Leu-Ile-Gln-Thr-Lys-Ile-Thr-Asp-Arg.
Background
What is the molecular weight/Mw of GLP 2 HUMAN Protein?
GLP 2 HUMAN Protein has a total Mw of 3.92kDa.

What is the Purity of GLP 2 HUMAN Protein?
GLP 2 HUMAN Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GLP 2 HUMAN Protein?
The biological functionality of GLP 2 HUMAN Protein will be determined in the future.

What is the amino acid sequence of GLP 2 HUMAN Protein?
His-Ala-Asp-Gly-Ser-Phe-Ser-Asp-Glu-Met-Asn-Thr-Ile-Leu-Asp-Asn-Leu-Ala-Ala-Arg-Asp-Phe-Ile-Asn-Trp-Leu-Ile-Gln-Thr-Lys-Ile-Thr-Asp-Arg.

What applications can GLP 2 HUMAN Protein be used in?
GLP 2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for GLP 2 HUMAN Protein?
The endotoxin level is minimal, GLP 2 HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

Ubiquitin Conjugating enzyme E2C Human Recombinant

Ubiquitin-conjugating enzyme E2 C, EC 6.3.2.19, Ubiquitin-protein ligase C, Ubiquitin carrier protein C, Ubc10, UBCH10, dJ447F3.2.

Product # :

ENZ-346

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Description

UBE2C Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 202 amino acids (1-179) and having a molecular mass of 22.1 kDa.The UBE2C is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

UBE2C protein 1mg/ml is supplied in 20mM Tris-HCL, pH-8, 0.15M NaCl, 1mM DTT and 10% Glycerol.

Purity

Greater than 90.0% as determined by Analysis by SDS-PAGE.

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Introduction
UbcH10 is an essential mediator of mitotic destruction events and cell cycle progression. It catalyzes the destruction of cyclins A and B in conjunction with the anaphase-promoting complex, and therefore, plays an important role in the control of the cell exit from mitosis This activity is essential at then end of mitosis for the inactivation of their partner kinase Cdc2 and exit from mitosis into G1 of the next cell cycle. In addition, UbcH10 bears homology to yeast PAS2, a gene that is essential for biogenesis of peroxisomes. UbcH10 is useful for in vitro ubiquitinylation reactions.
Synonyms
Ubiquitin-conjugating enzyme E2 C, EC 6.3.2.19, Ubiquitin-protein ligase C, Ubiquitin carrier protein C, Ubc10, UBCH10, dJ447F3.2.
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 MGSMASQNRD PAATSVAAAR KGAEPSGGAA RGPVGKRLQQ ELMTLMMSGD KGISAFPESD NLFKWVGTIH GAAGTVYEDL RYKLSLEFPS GYPYNAPTVK FLTPCYHPNV DTQGNICLDI LKEKWSALYD VRTILLSIQS LLGEPNIDSP LNTHAAELWK NPTAFKKYLQ ETYSKQVTSQ EP

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:

IFN-Beta 1a Human Recombinant

Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1a ,MGC96956.

Product # :

CYT-236

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Description

IFN-beta 1a Human Recombinant produced in CHO (Chinese Hamster Ovarian) cells is a single, glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 22500 Dalton.IFN-beta1a is purified by proprietary chromatographic techniques.

Source

CHO (Chinese Hamster Ovarian) cells.

Formulation

Lyophilized from a solution containing 91 mg Human Albumin, and 620 mg mannitol and 50mM Acetate acid pH 3.8.

Purity

Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.

Biological Activity

The specific activity as determined in a viral resistance assay (human "Wish" cell line and VSV virus or the monkey VERO cell line with EMCV virus) was found to be 270 x 10⁶ IU/mg.

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Introduction
IFN-beta has antiviral, antibacterial and anticancer activities.
Synonyms
Leukocyte IFN, B cell IFN, Type I IFN, IFNB1, IFB, IFF, IFNB, IFN-b 1a ,MGC96956.
Stability
Lyophilized IFN-beta 1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-Beta1a 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 IFN beta 1a in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Background
What is the molecular weight/Mw of IFN BETA 1A HUMAN Protein?
IFN BETA 1A HUMAN Protein has a total Mw of 22.5kDa.

What is the source or expression system of IFN BETA 1A HUMAN Protein?
CHO (Chinese Hamster Ovarian) cells.

What is the Purity of IFN BETA 1A HUMAN Protein?
IFN BETA 1A HUMAN Protein is >99% pure as determined by SDS-PAGE.

What is the Biological Activity of IFN BETA 1A HUMAN Protein?
The specific activity as determined in a viral resistance assay (human "Wish" cell line and VSV virus or the monkey VERO cell line with EMCV virus) was found to be 270 x 106 IU/mg.

What is the amino acid sequence of IFN BETA 1A HUMAN Protein?
IFN BETA 1A HUMAN Protein is composed from 166 amino acids.

What applications can IFN BETA 1A HUMAN Protein be used in?
IFN BETA 1A HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IFN BETA 1A HUMAN Protein?
The endotoxin level is minimal, IFN BETA 1A HUMAN Protein was purified using conventional chromatography techniques.

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

Description:

Proteasome Subunit Beta Type 3 Human Recombinant

Proteasome (prosome, macropain) subunit beta type 3, Proteasome chain 13, HC10-II, Proteasome component C10-II, Proteasome theta chain, EC 3.4.25.1, MGC4147.

Product # :

ENZ-200

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Description

PSMB3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-205 a.a.) and having a molecular mass of 25.1kDa.PSMB3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PSMB3 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 200mM NaCl, 1mM DTT and 50% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
The proteasome is a multicatalytic proteinase complex with an extremely organized ring-shaped 20S core structure. The core structure consists of 4 rings of 28 non-identical subunits; 2 rings consist of 7 alpha subunits and 2 rings consist of 7 beta subunits. Proteasomes are spread all over the eukaryotic cells in large quantities and cleave peptides in an ATP/ubiquitin-dependent procedure in a non-lysosomal pathway. A vital role of a modified proteasome, the immunoproteasome, is the handling of class I MHC peptides.
Synonyms
Proteasome (prosome, macropain) subunit beta type 3, Proteasome chain 13, HC10-II, Proteasome component C10-II, Proteasome theta chain, EC 3.4.25.1, MGC4147.
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 MSIMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY IGLAGLATDV QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF GPYYTEPVIA GLDPKTFKPF ICSLDLIGCP MVTDDFVVSG TCAEQMYGMC ESLWEPNMDP DHLFETISQA MLNAVDRDAV SGMGVIVHII EKDKITTRTL KARMD

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:

Proteasome Subunit Beta Type 4 Human Recombinant

Proteasome (prosome, macropain) subunit beta type 4, PROS26, HN3, Macropain beta chain, Multicatalytic endopeptidase complex beta chain, Proteasome chain 3, 26 kDa prosomal protein, HsN3, PROS-26, hsBPROS26, EC 3.4.25.1.

Product # :

ENZ-197

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Description

PSMB4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 240 amino acids (46-264 a.a.) and having a molecular mass of 26.6kDa.PSMB4 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

PSMB4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 30% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
PSMB4 is a member of the peptidase T1B family. The 20S Proteasome chamber holds structural alpha subunits and predominantly catalytic beta subunits. The two external rings in the proteasome contain seven alpha subunits each and the two internal rings contain of seven beta subunits each. PSMB4 is a beta subunit of the 20S Proteasome that is spread all over the eukaryotic cells in large quantities and cleaves peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway.
Synonyms
Proteasome (prosome, macropain) subunit beta type 4, PROS26, HN3, Macropain beta chain, Multicatalytic endopeptidase complex beta chain, Proteasome chain 3, 26 kDa prosomal protein, HsN3, PROS-26, hsBPROS26, EC 3.4.25.1.
Physical Appearance
Sterile Filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTQNPMVTGT SVLGVKFEGG VVIAADMLGS YGSLARFRNI SRIMRVNNST MLGASGDYAD FQYLKQVLGQ MVIDEELLGD GHSYSPRAIH SWLTRAMYSR RSKMNPLWNT MVIGGYADGE SFLGYVDMLG VAYEAPSLAT GYGAYLAQPL LREVLEKQPV LSQTEARDLV ERCMRVLYYR DARSYNRFQI ATVTEKGVEI EGPLSTETNW DIAHMISGFE

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:

Adaptor-Related Protein Complex 1, Sigma 2 Human Recombinant

Adaptor-related protein complex 1 sigma 2 subunit, SIGMA1B, Adaptor protein complex AP-1 sigma-1B subunit, Clathrin assembly protein complex 1 sigma-1B small chain, Golgi adaptor HA1/AP1 adaptin sigma-1B subunit, Sigma 1B subunit of AP-1 clathrin, MRX59, mental retardation X-linked 59, MGC:1902, AP-1 complex subunit sigma-2, golgi adaptor HA1/AP1 adaptin sigma 1B subunit.

Product # :

PRO-234

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Description

AP1S2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 177 amino acids (1-157a.a) and having a molecular mass of 20.7kDa.AP1S2 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

AP1S2 protein solution (0.5mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.1M NaCl and 2mM DTT.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
AP1S2 belongs to the adaptin protein family and functions as the small subunit of AP-1 complex 1 which is found in the cytoplasmic face of coated vesicles placed at the Golgi complex. AP-1 complex 1 facilitates both the necessity of clathrin to the membrane and the identification of organizing signals within the cytosolic tails of transmembrane receptors.
Synonyms
Adaptor-related protein complex 1 sigma 2 subunit, SIGMA1B, Adaptor protein complex AP-1 sigma-1B subunit, Clathrin assembly protein complex 1 sigma-1B small chain, Golgi adaptor HA1/AP1 adaptin sigma-1B subunit, Sigma 1B subunit of AP-1 clathrin, MRX59, mental retardation X-linked 59, MGC:1902, AP-1 complex subunit sigma-2, golgi adaptor HA1/AP1 adaptin sigma 1B subunit.
Physical Appearance
Sterile Filtered clear solution.
Stability
AP1S2 although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MQFMLLFSRQ GKLRLQKWYV PLSDKEKKKI TRELVQTVLA RKPKMCSFLE WRDLKIVYKR YASLYFCCAI EDQDNELITL EIIHRYVELL DKYFGSVCEL DIIFNFEKAY FILDEFLLGG EVQETSKKNV LKAIEQADLL QEEAETPRSV LEEIGLT

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:

SYF2 RNA splicing factor Human Recombinant

Pre-mRNA-splicing factor SYF2, CCNDBP1-interactor, p29, SYF2, CBPIN, GCIPIP, NTC31, fSAP29.

Product # :

PRO-969

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Description

SYF2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (94-243) and having a molecular mass of 20.5kDa.SYF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The SYF2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl, 5mM DTT and 2mM EDTA.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Pre-mRNA-splicing factor SYF2 (SYF2) may be involved in pre-mRNA splicing. The SYF2 protein interacts with cyclin D-type binding-protein 1, which is believed to be a cell cycle regulator at the G1/S transition. SYF2 is amply expressed in the heart, skeletal muscle and kidney and is expressed at lower levels in other tissues.
Synonyms
Pre-mRNA-splicing factor SYF2, CCNDBP1-interactor, p29, SYF2, CBPIN, GCIPIP, NTC31, fSAP29.
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 MGSDYEKVKL LEISAEDAER WERKKKRKNP DLGFSDYAAA QLRQYHRLTK QIKPDMETYE RLREKHGEEF FPTSNSLLHG THVPSTEEID RMVIDLEKQI EKRDKYSRRR PYNDDADIDY INERNAKFNK KAERFYGKYT AEIKQNLERG TAV.

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:

Crystallin, Gamma S Human Recombinant

Crystallin gamma S, Gamma-crystallin S, CRYG8, crystallin, gamma 8, Beta-crystallin S.

Product # :

PRO-963

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Description

CRYGS Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 202 amino acids (1-178) and having a molecular mass of 23.6 kDa.The CRYGS is fused to a 24 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

Source

E.coli.

Formulation

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

Purity

Greater than 95% as determined by SDS-PAGE.

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Introduction
Mammalian crystallins which are water soluble structural proteins located in the vertebrate eye are classified in three forms, labeled alpha, beta and gamma. Crystallins, the primary components of the lens, raise the refractive index of the eye all through the accommodation by creating high-molecular weight aggregates that maintain transparency. CRYGS is a monomer that does not aggregate. CRYGS encodes the most substantial gamma-crystallin in adult eye lens tissue. Gamma-crystallins has a part in cataract formation due to aging or mutations in specific genes,
Synonyms
Crystallin gamma S, Gamma-crystallin S, CRYG8, crystallin, gamma 8, Beta-crystallin S.
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 MGSHMSKTGT KITFYEDKNF QGRRYDCDCD CADFHTYLSR CNSIKVEGGT WAVYERPNFA GYMYILPQGE YPEYQRWMGL NDRLSSCRAV HLPSGGQYKI QIFEKGDFSG QMYETTEDCP SIMEQFHMRE IHSCKVLEGV WIFYELPNYR GRQYLLDKKE YRKPIDWGAA SPAVQSFRRI VE

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 13 Receptor Alpha 2, Recombinant Human Sf9

CD213A2, CT19, IL-13R, IL13BP, IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, CD_antigen=CD213a2, Interleukin-13-binding protein.

Product # :

CYT-1024

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Description

IL13RA2 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 559 amino acids (27-343 a.a.) and having a molecular mass of 64.3kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). IL13RA2 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL 13RA2 protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

Purity

Greater than 85.0% as determined by SDS-PAGE.

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Introduction
Interleukin 13 Receptor, Alpha 2 (IL13RA2) is a member of the type I cytokine receptor family, Type 5 subfamily. IL13RA2 is related to l13RA1, a subunit of the interleukin 13 receptor complex. IL13RA2 binds IL13 with high affinity, though lacking the cytoplasmic domain, and does not appear to function as a signal mediator. IL13RA2 plays a role in the internalization of IL13.
Synonyms
CD213A2, CT19, IL-13R, IL13BP, IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, CD_antigen=CD213a2, Interleukin-13-binding protein.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADLDTEIKVN PPQDFEIVDP GYLGYLYLQW QPPLSLDHFK ECTVEYELKY RNIGSETWKT IITKNLHYKD GFDLNKGIEA KIHTLLPWQC TNGSEVQSSW AETTYWISPQ GIPETKVQDM DCVYYNWQYL LCSWKPGIGV LLDTNYNLFY WYEGLDHALQ CVDYIKADGQ NIGCRFPYLE ASDYKDFYIC VNGSSENKPI RSSYFTFQLQ NIVKPLPPVY LTFTRESSCE IKLKWSIPLG PIPARCFDYE IEIREDDTTL VTATVENETY TLKTTNETRQ LCFVVRSKVN IYCSDDGIWS EWSDKQCWEG EDLSKKTLLR LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN
HYTQKSLSLS PGKHHHHHH
Background
What is the molecular weight/Mw of IL13RA2 HUMAN, SF9 Protein?
IL13RA2 HUMAN, SF9 Protein has a total Mw of 64.3kDa.

What is the source or expression system of IL13RA2 HUMAN, SF9 Protein?
Sf9, Baculovirus cells.

What is the Purity of IL13RA2 HUMAN, SF9 Protein?
IL13RA2 HUMAN, SF9 Protein is >85% pure as determined by SDS-PAGE.

What is the Biological Activity of IL13RA2 HUMAN, SF9 Protein?
The biological functionality of IL13RA2 HUMAN, SF9 Protein will be determined in the future.

What is the amino acid sequence of IL13RA2 HUMAN, SF9 Protein?
ADLDTEIKVN PPQDFEIVDP GYLGYLYLQW QPPLSLDHFK ECTVEYELKY RNIGSETWKT IITKNLHYKD GFDLNKGIEA KIHTLLPWQC TNGSEVQSSW AETTYWISPQ GIPETKVQDM DCVYYNWQYL LCSWKPGIGV LLDTNYNLFY WYEGLDHALQ CVDYIKADGQ NIGCRFPYLE ASDYKDFYIC VNGSSENKPI RSSYFTFQLQ NIVKPLPPVY LTFTRESSCE IKLKWSIPLG PIPARCFDYE IEIREDDTTL VTATVENETY TLKTTNETRQ LCFVVRSKVN IYCSDDGIWS EWSDKQCWEG EDLSKKTLLR LEPKSCDKTH TCPPCPAPEL LGGPSVFLFP PKPKDTLMIS RTPEVTCVVV DVSHEDPEVK FNWYVDGVEV HNAKTKPREE QYNSTYRVVS VLTVLHQDWL NGKEYKCKVS NKALPAPIEK TISKAKGQPR EPQVYTLPPS RDELTKNQVS LTCLVKGFYP SDIAVEWESN GQPENNYKTT PPVLDSDGSF FLYSKLTVDK SRWQQGNVFS CSVMHEALHN
HYTQKSLSLS PGKHHHHHH.

What applications can IL13RA2 HUMAN, SF9 Protein be used in?
IL13RA2 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for IL13RA2 HUMAN, SF9 Protein?
The endotoxin level is minimal, IL13RA2 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

Who supplies recombinant IL13RA2 HUMAN, SF9 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 IL13RA2 HUMAN, SF9?
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:

Laforin, Mouse Anti Human

Laforin, Lafora PTPase, LAFPTPase, EPM2A, EPM2, MELF, epilepsy progressive myoclonus type 2A Lafora disease.

Product # :

ANT-427

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Formulation

1mg/ml containing PBS, pH-7.4, & 0.1% Sodium Azide.

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Introduction
EPM2A is a dual-specificity phosphatase which associates with polyribosomes. The EPM2A protein may be involved in the regulation of glycogen metabolism. Mutations in the EPM2A gene have been linked to myoclonic epilepsy of Lafora.
Synonyms
Laforin, Lafora PTPase, LAFPTPase, EPM2A, EPM2, MELF, epilepsy progressive myoclonus type 2A Lafora disease.
Immunogen
Anti-human EPM2A mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with recombinant human EPM2A amino acids 243-331 purified from E. coli.
Ig Subclass
Mouse IgG1 heavy chain and κ light chain.
Clone
P3F3AT.
Applications
EPM2A antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results. Recommended dilution range for Western blot analysis is 1:1,000 ~ 2,000. Recommended starting dilution is 1:1,000.
Type
Mouse Anti Human Monoclonal.
Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
Purification Method
EPM2A antibody was purified from mouse ascitic fluids by protein-G affinity chromatography.

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

Description:

Glycine-N-Acyltransferase-Like 2 Human Recombinant

BXMAS2-10, GATF-B, Glycine N-acyltransferase-like protein 2, Acyl-CoA:glycine N-acyltransferase-like protein 2, GLYATL2.

Product # :

ENZ-770

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Description

GLYATL2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 317 amino acids (1-294a.a) and having a molecular mass of 36.7kDa. GLYATL2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GLYATL2 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 50% glycerol and 2mM DTT.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Glycine-N-Acyltransferase-Like 2 (GLYATL2) is a part of the glycine N-acyltransferase family expressed mainly in salivary gland and trachea. GLYATL2 is a mitochondrial acyltransferase that transfers the acyl group to the N-terminus of glycine. GLYATL2 conjugates numerous substrates, like arachidonoyl-CoA and saturated medium and longchain acyl-CoAs ranging from chain-length C8:0-CoA to C18:0-CoA, to form a variety of N-acylglycines. GLYATL2 also shows a preference for monounsaturated fatty acid oleoyl-CoA (C18:1-CoA) as an acyl donor.
Synonyms
BXMAS2-10, GATF-B, Glycine N-acyltransferase-like protein 2, Acyl-CoA:glycine N-acyltransferase-like protein 2, GLYATL2.
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 MGSMLVLHNS QKLQILYKSL EKSIPESIKV YGAIFNIKDK NPFNMEVLVD AWPDYQIVIT RPQKQEMKDD QDHYTNTYHI FTKAPDKLEE VLSYSNVISW EQTLQIQGCQ EGLDEAIRKV ATSKSVQVDY MKTILFIPEL PKKHKTSSND KMELFEVDDD NKEGNFSNMF LDASHAGLVN EHWAFGKNER SLKYIERCLQ DFLGFGVLGP EGQLVSWIVM EQSCELRMGY TVPKYRHQGN MLQIGYHLEK YLSQKEIPFY FHVADNNEKS LQALNNLGFK ICPCGWHQWK CTPKKYC.

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:

Transforming Growth Factor Beta Receptor I Human Recombinant

TGFBR1, AAT5, ACVRLK4, ALK-5, ALK5, ESS1, LDS1, LDS1A, LDS2A, MSSE, SKR4, tbetaR-I, TGFR-1.

Product # :

PKA-111

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Description

TGFBR1produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 342 amino acids (27-126a.a.) and having a molecular mass of 38.0kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).TGFBR1is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

TGFBR1protein solution (0.5mg/ml) Phosphate Buffered Saline (pH 7.4) containing 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
TGFBR1 is a single-pass type 1 membrane protein which is a part of the TGFB receptor subfamily and the protein kinase superfamily. TGFBR1 is a secreted protein that performs many cellular functions such as the control of cell growth, cell differentiation, cell proliferation and apoptosis. TGFBR1 also controls the immune system and shows different activities on various types of cell, or cells at different developmental stages.
Synonyms
TGFBR1, AAT5, ACVRLK4, ALK-5, ALK5, ESS1, LDS1, LDS1A, LDS2A, MSSE, SKR4, tbetaR-I, TGFR-1.
Physical Appearance
Sterile filtered colorless solution.
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
Amino Acid Sequence
ADLLLPGATA LQCFCHLCTK DNFTCVTDGL CFVSVTETTD KVIHNSMCIA EIDLIPRDRP FVCAPSSKTG SVTTTYCCNQ DHCNKIELPT TVKSSPGLGP VELVEPKSCD KTHTCPPCPA PELLGGPSVF LFPPKPKDTL MISRTPEVTC VVVDVSHEDP EVKFNWYVDG VEVHNAKTKP REEQYNSTYR VVSVLTVLHQ DWLNGKEYKC KVSNKALPAP IEKTISKAKG QPREPQVYTL PPSRDELTKN QVSLTCLVKG FYPSDIAVEW ESNGQPENNY KTTPPVLDSD GSFFLYSKLT VDKSRWQQGN VFSCSVMHEA LHNHYTQKSL SLSPGKHHHH HH.

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:

Non-Metastatic Cells 2 Human Recombinant

Nucleoside diphosphate kinase B, NDPK-B, NDPKB, NM23-H2, NM23B, EC 2.7.4.6, NDP kinase B, C-myc purine-binding transcription factor PUF, NDK B, NME2, puf, MGC111212.

Product # :

PKA-363

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Description

NME2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids (1-152 a.a.) and having a molecular mass of 17.2kDa. The NME2 is purified by conventional chromatography.

Source

Escherichia Coli.

Formulation

The NME2 protein solution contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
NME2 takes an important part in the synthesis of nucleoside triphosphates other than ATP. NME2 negatively controls Rho activity by interacting with AKAP13/LBC. NME2 acts as a transcriptional activator of the MYC gene. NME2 binds DNA non-specifically. NME2 is a heterodimeric enzyme functioning as a nucleoside diphosphate kinase. NME1 and NME2 contain 152 amino acids, A and B polypeptide chains of the NM23 enzyme, respectively. NME2 is identical to the beta subunit of human erythrocyte NDP kinase. NDP kinases participate in the synthesis of nucleoside triphosphates, and NM23 is involved in the regulation of signal transduction by complexing with G proteins, causing activation/inactivation of developmental pathways.
Synonyms
Nucleoside diphosphate kinase B, NDPK-B, NDPKB, NM23-H2, NM23B, EC 2.7.4.6, NDP kinase B, C-myc purine-binding transcription factor PUF, NDK B, NME2, puf, MGC111212.
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
MANLERTFIA IKPDGVQRGL VGEIIKRFEQ KGFRLVAMKF LRASEEHLKQ HYIDLKDRPF FPGLVKYMNS GPVVAMVWEG LNVVKTGRVM LGETNPADSK PGTIRGDFCI QVGRNIIHGS DSVKSAEKEI SLWFKPEELV DYKSCAHDWV YE.

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:

MIG Mouse Recombinant (CXCL9)

Small inducible cytokine B9, CXCL9, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, M119.

Product # :

CHM-337

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Description

MIG (CXCK9) Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 105 amino acids and having a molecular mass of 12208 Dalton. The MIG is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Filtered (0.2µm) and lyophilized from a concentrated (0.5mg/ml) solution in 20mM PB, pH7.4 and 100mM NaCl.

Purity

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

Biological Activity

The Activity is calculated by the ability to chemoattract Human lymphocytes using a concentration of 0.1-1 ng/ml.

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Introduction
Chemokine (C-X-C motif) ligand 9 (CXCL9) is a small cytokine belonging to the CXC chemokine family that is also known as Monokine induced by MIG. CXCL9 is a T-cell chemoattractant. It is closely related to two other CXC chemokines called CXCL10 and CXCL11, whose genes are located near the gene for CXCL9 on human chromosome 4. CXCL9, CXCL10 and CXCL11 all elicit their chemotactic functions by interacting with the chemokine receptor CXCR3.
Synonyms
Small inducible cytokine B9, CXCL9, MIG, chemokine (C-X-C motif) ligand 9, CMK, Humig, SCYB9, crg-10, M119.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized MIG although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL9 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 MIG in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
TLVIRNARCS CISTSRGTIH YKSLKDLKQF APSPNCNKTE IIATLKNGDQ TCLDPDSANV KKLMKEWEKK INQKKKQKRG KKHQKNMKNR KPKTPQSRRR SRKTT.
Background
What is the molecular weight/Mw of CXCL9 MOUSE Protein?
CXCL9 MOUSE Protein has a total Mw of 12.2kDa.

What is the source or expression system of CXCL9 MOUSE Protein?
Escherichia Coli.

What is the Purity of CXCL9 MOUSE Protein?
CXCL9 MOUSE Protein is > 97% pure as determined by SDS-PAGE.

What is the Biological Activity of CXCL9 MOUSE Protein?
The Activity is calculated by the ability to chemoattract Human lymphocytes using a concentration of 0.1-1 ng/ml.

What is the amino acid sequence of CXCL9 MOUSE Protein?
TLVIRNARCS CISTSRGTIH YKSLKDLKQF APSPNCNKTE IIATLKNGDQ TCLDPDSANV KKLMKEWEKK INQKKKQKRG KKHQKNMKNR KPKTPQSRRR SRKTT.

What applications can CXCL9 MOUSE Protein be used in?
CXCL9 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for CXCL9 MOUSE Protein?
The endotoxin level is minimal, CXCL9 MOUSE Protein was purified using conventional chromatography techniques.
Who supplies recombinant CXCL9 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 CXCL9 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:

Lipopolysaccharide-Induced TNF Factor Human Recombinant

Lipopolysaccharide-induced TNF-alpha factor, PIG7, SIMPLE, Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF.

Product # :

PRO-1350

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Description

LITAF Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 181 amino acids (1-161) and having a molecular mass of 19.2 kDa. LITAF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The LITAF solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M Urea and 10% glycerol.

Purity

Greater than 85% as determined by SDS-PAGE.

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Introduction
Lipopolysaccharide-induced TNF-alpha factor (LITAF) is a small integral membrane protein of lysosome/late endosome. The expression of inflammatory cytokines such as TNF-alpha in Lipopolysaccharide-induced processes is mediated by LITAF. LITAF connects to STAT6B, which belongs to the STAT6 family forming a complex on the TNF-alpha promoter that modifies TNF activity. High levels of expression of LITAF mRNA are observed mostly in the placenta, peripheral blood leukocytes, lymph nodes and spleen.
Synonyms
Lipopolysaccharide-induced TNF-alpha factor, PIG7, SIMPLE, Lipopolysaccharide-induced tumor necrosis factor-alpha factor, LPS-induced TNF-alpha factor, p53-induced gene 7 protein, Small integral membrane protein of lysosome/late endosome, LITAF.
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 MSVPGPYQAA TGPSSAPSAP PSYEETVAVN SYYPTPPAPM PGPTTGLVTG PDGKGMNPPS YYTQPAPIPN NNPITVQTVY VQHPITFLDR PIQMCCPSCN KMIVSQLSYN AGALTWLSCG SLCLLGCIAG CCFIPFCVDA LQDVDHYCPN CRALLGTYKR L.

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:

Polyclonal Rabbit Anti Dengue 2 NS1

Product # :

ANT-084

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Description

The polyclonal antibody to dengue serotype 2 NS1 was collected from the rabbit immunized with full length recombinant dengue serotype 2 NS1 antigen.

Formulation

PBS + 0.02% sodium azide.

Purity

Protein is >90% pure.

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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.
Purification Method
Purified by affinity 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.

Description:

Solute Carrier Family 51 Beta Human Recombinant

OSTB, OSTBETA, Organic solute transporter subunit beta, OST-beta, Solute carrier family 51 subunit beta.

Product # :

PRO-1727

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Description

SLC51B Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (57-128 a.a) and having a molecular mass of 10.7kDa.SLC51B is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

SLC51B protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
Solute Carrier Family 51 Beta (SLC51B), is a protein coding gene. SLC51B is an organic solute transporter subunit. SLC51 is composed of twodifferent proteins that must heterodimerize to generate transport activity, however the role of the individual subunits inmediating transport activity is unknown. The results show that SLC51B is required for both proper traffickingof SLC51A and formation of the functional transport unit, and identify specific residues of SLC51B essential for theseprocesses. Among the diseases associated with SLC51B are extrahepatic cholestasis, and biliary atresia.
Synonyms
OSTB, OSTBETA, Organic solute transporter subunit beta, OST-beta, Solute carrier family 51 subunit beta.
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 MGSRSIQASR KEKMQPPEKE TPEVLHLDEA KDHNSLNNLR ETLLSEKPNL AQVELELKER DVLSVFLPDV PETES

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-17 Receptor Beta Mouse Recombinant

Il17rb, Evi27, IL-17ER, IL-17Rh1, Il17br, IL17RH1, IL-17 receptor B, IL-17RB, Interleukin-17 receptor B.

Product # :

CYT-960

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Description

IL17RB produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 511 amino acids (18-286 a.a.) and having a molecular mass of 57.1kDa (Molecular size on SDS-PAGE will appear at approximately 57-70kDa). IL17RB is expressed with an 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

Source

Sf9, Baculovirus cells.

Formulation

IL17RB protein solution (1mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
IL17 is a proinflammatory cytokine produced by activated T cells. IL-17 regulates the activities of NF-kappaB and mitogen-activated protein kinases. Interleukin-17 can stimulate the expression of IL6 and cyclooxygenase-2 (PTGS2/COX-2), as well as enhance the production of nitric oxide (NO). High levels of IL-17 are associated with several chronic inflammatory diseases including rheumatoid arthritis, psoriasis and multiple sclerosis.
Synonyms
Il17rb, Evi27, IL-17ER, IL-17Rh1, Il17br, IL17RH1, IL-17 receptor B, IL-17RB, Interleukin-17 receptor B.
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
ADPREPTIQC GSETGPSPEW MVQHTLTPGD LRDLQVELVK TSVAAEEFSI LMNISWILRA DASIRLLKAT KICVSGKNNM NSYSCVRCNY TEAFQSQTRP SGGKWTFSYV GFPVELSTLY LISAHNIPNA NMNEDSPSLS VNFTSPGCLN HVMKYKKQCT EAGSLWDPDI TACKKNEKMV EVNFTTNPLG NRYTILIQRD TTLGFSRVLE NKLMRTSVAI PVTEESEGAV VQLTPYLHTC GNDCIRREGT VVLCSETSAP IPPDDNRRML GGVEPKSCDK THTCPPCPAP ELLGGPSVFL FPPKPKDTLM ISRTPEVTCV VVDVSHEDPE VKFNWYVDGV EVHNAKTKPR EEQYNSTYRV VSVLTVLHQD WLNGKEYKCK VSNKALPAPI EKTISKAKGQ PREPQVYTLP PSRDELTKNQ VSLTCLVKGF YPSDIAVEWE SNGQPENNYK TTPPVLDSDG SFFLYSKLTV DKSRWQQGNV FSCSVMHEAL HNHYTQKSLS LSPGKHHHHH 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:

Activin-A Human Recombinant, Active

Inhba, Inhibin beta A, FSH releasing protein.

Product # :

CYT-145

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Description

Active form Activin-A Human Recombinant produced in e.coli is a homodimeric, non-glycosylated, polypeptide chain containing 2 x 117 amino acids and having a molecular weight of 26.2kDa.The Active form Activin-A is purified by standard chromatographic techniques.

Source

E.Coli.

Formulation

Human Activin-A was lyophilized from a concentrated 1mg/ml protein solution containing 0.1% TFA.

Purity

Greater than 95% as obsereved by SDS-PAGE.

Biological Activity

Biological activity is assessed by the ability to induce cytotoxicity of MPC-11 cells and was found to be 8.95ng/ml corresponding to a specific activity of 1.1 x 10⁵ units/mg.

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Introduction
Activins are homodimers or heterodimers of the different β subunit isoforms, part of the TGFβ family. Mature Activin A has two 116 amino acids residues βA subunits (βA-βA). Activin displays an extensive variety of biological activities, including mesoderm induction, neural cell differentiation, bone remodelling, haematopoiesis, and reproductive physiology. Activins takes part in the production and regulation of hormones such as FSH, LH, GnRH and ACTH. Cells that are identified to express Activin A include fibroblasts, endothelial cells, hepatocytes, vascular smooth muscle cells, macrophages, keratinocytes, osteoclasts, bone marrow monocytes, prostatic epithelium, neurons, chondrocytes, osteoblasts, Leydig cells, Sertoli cells, and ovarian granulosa cells.
Synonyms
Inhba, Inhibin beta A, FSH releasing protein.
Physical Appearance
Lyophilized freeze dried powder.
Stability
Lyophilized Activin-A although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Activin-A should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
Solubility
Human INHBA protein should be reconstituted in distilled pyrogen free water to a concentration of 100ug /ml which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MGLECDGKVN ICCKKQFFVS FKDIGWNDWI IAPSGYHANY CEGECPSHIA GTSGSSLSFH STVINHYRMR GHSPFANLKS CCVPTKLRPM SMLYYDDGQN IIKKDIQNMI VEECGCS.
Background
Title: Research on Activin A Human Recombinant: Molecular Characteristics, Signaling Pathways, Physiological Functions, and Therapeutic Potential
Introduction:
Activin A, a member of the transforming growth factor-beta (TGF-β) superfamily, is a multifunctional cytokine that plays a significant role in various biological processes in the human body. Its involvement in diverse physiological and pathological functions has garnered considerable attention in scientific research. This paper aims to provide an overview of Activin A, encompassing its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential.
Activin A is encoded by the INHBA gene and is produced as a precursor protein that undergoes post-translational modifications to generate the mature form. The mature Activin A protein consists of two β-subunits held together by disulfide bonds. These structural features contribute to its functional properties and interactions with specific receptors.
Upon binding to its cell surface receptors, Activin A triggers intracellular signaling cascades, leading to various cellular responses. Canonical SMAD-dependent pathway as well as non-SMAD pathways, such as MAPK/ERK, PI3K/Akt, and JNK signaling, are activated by Activin A. The intricate network of signaling pathways enables Activin A to regulate diverse biological processes, including cell proliferation, differentiation, apoptosis, and tissue homeostasis.
Activin A exerts its physiological functions in a tissue-specific manner. It plays a critical role in embryonic development, particularly in organogenesis and patterning. Additionally, Activin A is involved in reproductive biology, where it participates in folliculogenesis, spermatogenesis, and hormonal regulation. It also contributes to neural development, immune system modulation, and skeletal homeostasis.
The multifunctional properties of Activin A have positioned it as a potential therapeutic target for various diseases. Its involvement in cancer, neurodegenerative disorders, fibrosis, and reproductive disorders has prompted extensive research to explore its therapeutic potential. Understanding the molecular mechanisms underlying Activin A's actions provides valuable insights for developing innovative therapeutic strategies.
In conclusion, Activin A is a versatile cytokine with diverse roles in human biology. This research aims to deepen our understanding of its molecular characteristics, signaling pathways, physiological functions, and therapeutic potential. By elucidating the complexities of Activin A, we strive to pave the way for novel therapeutic interventions in various human diseases.

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:

Epstein Barr Virus Induced 3 Macaque Recombinant

IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.

Product # :

CYT-1036

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Description

EBI3 Macaque Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 210 amino acids and having a molecular mass of 23.4kDa. The EBI3 is purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

Lyophilized from a sterile filtered solution containing 0.1 % trifluoroacetic acid (TFA).

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
EBI3 has an induced expression in B lymphocytes in reaction to Epstein-Barr virus infection. EBI3 encodes a secreted glycoprotein belonging to the hematopoietin receptor family, and heterodimerizes with a 28 kDa protein to form iIL-27. EBI3 drives rapid clonal expansion of naive cd4(+) t-cells. EBI3 strongly synergizes with IL-12 to activate IFN-gamma production of naive cd4(+) t-cells. EBI3 mediates its biologic effects through the cytokine receptor wsx-1/tccr.
Synonyms
IL-27B, IL27B, IL 27-B, EBI-3, Interleukin-27 beta, IL-27 subunit beta, Epstein-Barr virus-induced gene 3 protein homolog, EBI3.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized EBI3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution EBI3 Macaque 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 EBI3 in sterile 18MΩ-cm H2O at a concentration of 100µg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
MRKGPPAALT LPRVQCRAPR YPIAVDCSWT LPPAPNSTSP VSFIATYRFG MAARGHSWPC LQQTPASTSC TIADVRLFSM APYVLNVTAV HPWGSSSSFV PFIAEHIIKP DPPEGVRLSP LAERQLQVQW EPPRSWPFPE IFSLKYWIRY KRQGAARFHQ VGPIEATSFI LRAVRPRARY CVQVAAQDLT DYGELSDWSL PATTPMSPGK.
Background
What is the molecular weight/Mw of EBI3 Protein?
EBI3 Protein has a total Mw of 23.4kDa.

What is the source or expression system of EBI3 Protein?
Escherichia Coli.

What is the Purity of EBI3 Protein?
EBI3 Protein is >90% pure as determined by SDS-PAGE.

What is the Biological Activity of EBI3 Protein?
The biological functionality of EBI3 Protein will be determined in the future.

What is the amino acid sequence of EBI3 Protein?
MRKGPPAALT LPRVQCRAPR YPIAVDCSWT LPPAPNSTSP VSFIATYRFG MAARGHSWPC LQQTPASTSC TIADVRLFSM APYVLNVTAV HPWGSSSSFV PFIAEHIIKP DPPEGVRLSP LAERQLQVQW EPPRSWPFPE IFSLKYWIRY KRQGAARFHQ VGPIEATSFI LRAVRPRARY CVQVAAQDLT DYGELSDWSL PATTPMSPGK.

What applications can EBI3 Protein be used in?
EBI3 Protein can probably be used in western blot, ELISA and Lateral Flow.

What is the endotoxin level for EBI3 Protein?
The endotoxin level is minimal, EBI3 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:

Immunoglobulin Heavy Chain Constant Region Gamma 2a Mouse Recombinant, His Tag

Ig gamma-2A chain C region, A allele, Immunoglobulin heavy chain gamma polypeptide, Ighg, Igh-1, Igh-1a, 1810060O09Rik.

Product # :

PRO-1086

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Description

IgG Mouse Recombinant produced in Hi-5 cells is a single polypeptide chain containing 242 amino acids (98-330 a.a) and having a molecular mass of 27.5kDa.IgG is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Source

Hi-5 cells.

Formulation

IgG protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

Purity

Greater than 90.0% as determined by SDS-PAGE.

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Introduction
Immunoglobulin G (IgG) are antibody molecules. Each IgG is composed of four peptide chains - 2 heavy chains g and 2 light chains. Also, each IgG has 2 antigen binding sites. IgG antibodies are involved in primarily the secondary immune response. The presence of specific IgG, generally, relates to maturation of the antibody response. IgG also has an imperative role in Antibody-dependent cell-mediated cytotoxicity (ADCC) and Intracellular antibody-mediated proteolysis, in which it binds to TRIM21 (the receptor with greatest affinity to IgG in humans) in order to direct marked virions to the proteasome in the cytosol.
Synonyms
Ig gamma-2A chain C region, A allele, Immunoglobulin heavy chain gamma polypeptide, Ighg, Igh-1, Igh-1a, 1810060O09Rik.
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
ADPEPRGPTI KPCPPCKCPA PNLLGGPSVF IFPPKIKDVL MISLSPIVTC VVVDVSEDDP DVQISWFVNN VEVHTAQTQT HREDYNSTLR VVSALPIQHQ DWMSGKEFKC KVNNKDLPAP IERTISKPKG SVRAPQVYVL PPPEEEMTKK QVTLTCMVTD FMPEDIYVEW TNNGKTELNY
KNTEPVLDSD GSYFMYSKLR VEKKNWVERN SYSCSVVHEG LHNHHTTKSF SRTPGKHHHH HH.

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:

Growth and Differentiation Factor 15 Human Recombinant, His Tag

GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.

Product # :

CYT-691

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Description

Recombinant Human GDF15 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 151 amino acids (195-308) and having a molecular mass of 16.7 kDa(molecular weight on SDS-PAGE will appear higher).GDF15 is expressed with a 36 amino acid His tag fused at N-Terminus and purified by proprietary chromatographic techniques.

Source

Escherichia Coli.

Formulation

The GDF15 protein solution contains 10mM sodium citrate, pH-3.5 & 10% glycerol.

Purity

Greater than 95.0% as determined by SDS-PAGE.

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Introduction
GDF15 is part of the TGF-Beta superfamily that is involved in regulating inflammatory and apoptotic pathways in injured tissues and throughout disease processes. GDF15 is most abundant in the liver. Its expression in liver can be considerably up-regulated in during injury of organs such as liver, kidney, heart and lung. GDF-15 promotes proliferation or growth arrest and differentiation due to differences in cellular differentiation. GDF15 prevents apoptosis in cerebellar granule neurons by activating Akt and inhibiting endogenously active ERK. GDF15 is a novel autocrine/endocrine factor that antagonizes the hypertrophic response and loss of ventricular performance.
Synonyms
GDF-15, MIC1, MIC-1, NAG-1, PDF, PLAB, PTGFB, Growth/differentiation factor 15, Placental bone morphogenetic protein, Placental TGF-beta, Macrophage inhibitory cytokine 1, Prostate differentiation factor, NSAID-activated gene 1 protein, NSAID-regulated gene 1 protein, NRG-1, GDF15.
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
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.
Background
What is the molecular weight/Mw of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein has a total Mw of 16.7kDa.

What is the source or expression system of GDF15 HUMAN, HIS Protein?
Escherichia Coli.

What is the Purity of GDF15 HUMAN, HIS Protein?
GDF15 HUMAN, HIS Protein is >95% pure as determined by SDS-PAGE.

What is the Biological Activity of GDF15 HUMAN, HIS Protein?
The biological functionality of GDF15 HUMAN, HIS Protein will be determined in the future.

What is the amino acid sequence of GDF15 HUMAN, HIS Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMARA RNGDHCPLGP GRCCRLHTVR ASLEDLGWAD WVLSPREVQV TMCIGACPSQ FRAANMHAQI KTSLHRLKPD TVPAPCCVPA SYNPMVLIQK TDTGVSLQTY DDLLAKDCHC I.

What applications can GDF15 HUMAN, HIS Protein be used in?
GDF15 HUMAN, HIS Protein can probably be used in western blot, ELISA and
Lateral Flow.

What is the endotoxin level for GDF15 HUMAN, HIS Protein?
The endotoxin level is minimal, GDF15 HUMAN, 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:

Staphylococcal Protein-A Cys Long Form Recombinant

Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.

Product # :

PRO-1924

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Description

SPA-Cys long Recombinant produced in E.Coli is a single non-glycosylated polypeptide chain with a Cys on C-terminus. SPA-Cys is comprised of 5 IgG-binding domains E-D-A-B-C aligned in series containing 423 amino acids and having a molecular mass of 46.7kDa containing little or no carbohydrate.

Source

Escherichia Coli.

Formulation

SPA protein was lyophilized with no additives.

Purity

Greater than 97.0% as determined by analysis by SDS-PAGE.

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Introduction
Protein A is a cell wall component produced by several strains of Staphylococcus aureus. The recombinant Protein A is genetically engineered protein and holds 5 IgG-binding regions of protein A. Recombinant Protein A functions basically the same as native Protein A and is perfect for purification of polyclonal or monoclonal IgG antibodies. Protein A binds to human IgG1, IgG2 and IgG4, mouse IgG2a, IgG2b and IgG3 and rat IgG2c. Protein A also binds to total IgG from rabbit, pig, dog, cat, and guinea pig.
Synonyms
Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Stability
Lyophilized SPA although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SPA 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 SPA in sterile 18MΩ-cm H2O not less than 0.1mg/ml, which can then be further diluted to other aqueous solutions.
Amino Acid Sequence
AQHDEAQQNA FYQVLNMPNL NADQRNGFIQ SLKDDPSQSA NVLGEAQKLN DSQAPKADAQ QNNFNKDQQS AFYEILNMPN LNEAQRNGFI QSLKDDPSQS TNVLGEAKKL NESQAPKADN NFNKEQQNAF YEILNMPNLN EEQRNGFIQS LKDDPSQSAN LLSEAKKLNE SQAPKADNKF NKEQQNAFYE ILHLPNLNEE QRNGFIQSLK DDPSQSANLL AEAKKLNDAQ APKADNKFNK EQQNAFYEIL HLPNLTEEQR NGFIQSLKDD PSVSKEILAE AKKLNDAQAP KEEDNKKPGK EDGNKPGKED GNKPGKEDNK KPGKEDGNKP GKEDNNKPGK EDGNKPGKED NNKPGKEDGN KPGKEDGNKP GKEDGNGVHV VKPGDTVNDI AKANGTTADK IAADNKLADK NMIKPGQELV VDC

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:

Beta-Secretase 2 Mouse Recombinant, HEK

BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.

Product # :

ENZ-1188

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Description

BACE2 Mouse Recombinant produced in HEK293 Cells is a single, glycosylated, polypeptide chain (20-462 a.a) containing a total of 449 amino acids, having a molecular mass of 48.6 kDa. BACE2 Mouse is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.

Source

HEK293 Cells.

Formulation

BACE2 (0.25mg/ml) is filtered in 10% (w/v) glycerol and Phosphate-Buffered Saline pH 7.4.

Purity

Greater than 95.0% as determined by SDS-PAGE.

Biological Activity

Specific activity is > 20 pmol/min/ug in which one unit will convert 1.0pmole of Mca-SEVNLDAEFRK(Dnp)RR-NH2 to Mca- Pro-Leu-OH per minute at pH 3.5 at 25C.

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Synonyms
BAE2, CDA13, CEAP1, DRAP, ARP1, ASP1, ASP21, 1110059C24Rik, AEPLC, AI850424, ALP56, beta-site APPcleaving enzyme 2, beta-secretase 2, Aspartyl protease 1, Asp 1, Beta-site amyloid precursor protein cleaving enzyme 2, Memapsin-1, Membrane-associated aspartic protease 1, Theta-secretase.
Physical Appearance
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
AVPALAPAPF TLPLQVARAT NHRASAVPGL GTPELPRADG LALALEPVRA TANFLAMVDN LQGDSGRGYY LEMLIGTPPQ KVQILVDTGS SNFAVAGAPH SYIDTYFDSE SSSTYHSKGF DVTVKYTQGS WTGFVGEDLV TIPKGFNSSF LVNIATIFES ENFFLPGIKW NGILGLAYAA LAKPSSSLET FFDSLVAQAK IPDIFSMQMC GAGLPVAGSG TNGGSLVLGG IEPSLYKGDI
WYTPIKEEWY YQIEILKLEI GGQNLNLDCR EYNADKAIVD SGTTLLRLPQ KVFDAVVEAV ARTSLIPEFS DGFWTGAQLA CWTNSETPWA YFPKISIYLR DENASRSFRI TILPQLYIQP MMGAGFNYEC YRFGISSSTN ALVIGATVME GFYVVFDRAQ RRVGFAVSPC AEIEGTTVSE ISGPFSTEDI ASNCVPAQAL NEP HHHHHH.
Background
BACE2 protein, a member of the beta-secretase family, has gained attention as a key player in the pathogenesis of neurological disorders, particularly Alzheimer's disease. This research aims to explore the function and potential therapeutic implications of BACE2 protein in neurodegenerative conditions. Understanding the role of BACE2 protein can provide valuable insights into its significance as a therapeutic target for the development of novel treatment strategies.
Function of BACE2 Protein:
BACE2 is a transmembrane aspartic protease predominantly expressed in the central nervous system. It exhibits distinct cleavage activity on various protein substrates, including neuregulins, APP-like proteins, and TGF-β. Unlike its close homolog BACE1, BACE2 has been proposed to have non-amyloidogenic processing capabilities and has shown potential neuroprotective effects.
Implications of BACE2 Protein in Alzheimer's Disease:
Alzheimer's disease is characterized by the accumulation of amyloid-beta (Aβ) peptides in the brain, which are generated through the sequential cleavage of amyloid precursor protein (APP). BACE1 is primarily responsible for the cleavage of APP, leading to the production of toxic Aβ peptides. In contrast, BACE2 has been suggested to compete with BACE1, thereby reducing the levels of Aβ generation. This has led to speculation about the neuroprotective role of BACE2 and its potential as a therapeutic target for Alzheimer's disease.
BACE2 Protein and Neuronal Survival:
Emerging evidence suggests that BACE2 may play a role in promoting neuronal survival and function. Studies have shown that BACE2 deficiency leads to impaired synaptic plasticity, reduced dendritic branching, and altered neurotransmitter release. BACE2 has also been implicated in the regulation of axonal growth and guidance during development. These findings highlight the potential importance of BACE2 in maintaining neuronal integrity.
Association of BACE2 Protein with Other Neurological Disorders:
Apart from Alzheimer's disease, BACE2 has been implicated in other neurological conditions as well. Genetic studies have identified BACE2 gene variants associated with an increased risk of Parkinson's disease, suggesting its involvement in the pathogenesis of this disorder. Furthermore, BACE2 has been linked to the regulation of insulin signaling and glucose homeostasis, making it a potential target for diabetes-associated cognitive decline.
Therapeutic Implications of BACE2 Protein:
Given its potential neuroprotective effects and modulatory role in amyloid processing, BACE2 protein has emerged as a promising therapeutic target for neurodegenerative disorders. Strategies aimed at enhancing BACE2 activity or selectively activating BACE2-mediated non-amyloidogenic processing pathways hold promise for reducing amyloid pathology and preserving neuronal function. However, further research is needed to better understand the complex mechanisms underlying BACE2 function and to develop safe and effective therapeutic interventions.
Conclusion:
The investigation of BACE2 protein has provided valuable insights into its role in neurodegenerative diseases, particularly Alzheimer's disease. The potential neuroprotective effects and modulation of amyloid processing pathways by BACE2 make it an intriguing therapeutic target. Future studies should focus on unraveling the precise mechanisms by which BACE2 influences disease pathogenesis and developing strategies to harness its therapeutic potential. The exploration of BACE2 protein opens new avenues for the development of innovative treatment approaches for neurodegenerative disorders.

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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