Antigens

SARS-COV-2-RBD (P0DTC2.1)

SARS-CoV-2 is a member of the betacoronavirus genus and is closely related to SARS-CoV (Wrapp et al. 2020). In general, three structural proteins are associated with the viral envelope of corona viruses: a membrane protein (M), an envelope protein (E) and a spike protein (S). The spike protein consists of three segments: an ectodomain (including subunits S1 and S2), a transmembrane anchor and a short intracellular tail. The trimeric transmembrane spike glycoprotein (S) mediates the coronavirus entry by receptor binding and membrane fusion. It consists of two functional subunits named S1 and S2. S1 mediates binding to the host receptor and shows a high diversity among corona viruses. S2 induces fusion of the virus with the cellular membrane of the host and is conserved.

S is synthesized as a single-chain precursor and trimerizes upon folding. Corona virus S proteins include up to two protease cleavage sites, i.e. between the S1 and S2 subunits (S1/S2) and upstream of the fusion peptide (S2’) (Walls et al. 2017). To bind a host cell receptor, the receptor-binding domain (RBD) of S1 has do undergo hinge-like conformational movements resulting in hiding or exposing the determinants of receptor binding. SARS-CoV-2 RBD consist of 223 amino acids (Lan et al. 2020). Nine cysteine residues are found within the RBD resulting in four disulfide bonds. RBM is described as receptor binding motif containing most of the residues that bind to ACE2.

Expression

Komagataella phaffii

SARS-CoV-2 RBD is expressed as glycosylated protein ranging in size between 45-55 kDa. After digestion with PNGase F the protein appears just above 25 kDa correlating with its calculated molecular weight.

Click on our Protein Products and view corresponding SDS-PAGE gels and/or Western blots.

Protein Product

RBD

SARS-CoV-2 RBD wild type

(C-term 6xHis, Ni-NTA purified)

 

SDS-PAGE reduced and denatured. 

Gene Sequence

R
319
V
320
Q
321
P
322
T
323
E
324
S
325
I
326
V
327
R
328
F
329
P
330
N
331
I
332
T
333
N
334
L
335
C
336
P
337
F
338
G
339
E
340
V
341
F
342
N
343
A
344
T
345
R
346
F
347
A
348
S
349
V
350
Y
351
A
352
W
353
N
354
R
355
K
356
R
357
I
358
S
359
N
360
C
361
V
362
A
363
D
364
Y
365
S
366
V
367
L
368
Y
369
N
370
S
371
A
372
S
373
F
374
S
375
T
376
F
377
K
378
C
379
Y
380
G
381
V
382
S
383
P
384
T
385
K
386
L
387
N
388
D
389
L
390
C
391
F
392
T
393
N
394
V
395
Y
396
A
397
D
398
S
399
F
400
V
401
I
402
R
403
G
404
D
405
E
406
V
407
R
408
Q
409
I
410
A
411
P
412
G
413
Q
414
T
415
G
416
K
417
I
418
A
419
D
420
Y
421
N
422
Y
423
K
424
L
425
P
426
D
427
D
428
F
429
T
430
G
431
C
432
V
433
I
434
A
435
W
436
N
437
S
438
N
439
N
440
L
441
D
442
S
443
K
444
V
445
G
446
G
447
N
448
Y
449
N
450
Y
451
L
452
Y
453
R
454
L
455
F
456
R
457
K
458
S
459
N
460
L
461
K
462
P
463
F
464
E
465
R
466
D
467
I
468
S
469
T
470
E
471
I
472
Y
473
Q
474
A
475
G
476
S
477
T
478
P
479
C
480
N
481
G
482
V
483
E
484
G
485
F
486
N
487
C
488
Y
489
F
490
P
491
L
492
Q
493
S
494
Y
495
G
496
F
497
Q
498
P
499
T
500
N
501
G
502
V
503
G
504
Y
505
Q
506
P
507
Y
508
R
509
V
510
V
511
V
512
L
513
S
514
F
515
E
516
L
517
L
518
H
519
A
520
P
521
A
522
T
523
V
524
C
525
G
526
P
527
K
528
K
529
S
530
T
531
N
532
L
533
V
534
K
535
N
536
K
537
C
538
V
539
N
540
F
541
Sample Quantity and Formulation

Lyophilized protein preparation or protein solution.

Secreted crude protein from Komagataella phaffii strain (cell free), lyophilized or in a solution (10 mM KH2PO4/K2HPO4 at pH 7.4). Constructs contain a polyhistidine-tag and are Ni-NTA purified.

Price: 250,- € per 100 µg protein

Prices do not include VAT, additional taxes or fees might apply. Shipping fees will be charged. Products are for research only. No resale of products.

 

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    References

    Wrapp, D., Wang, N., Corbett, K. S., Goldsmith, J. A., Hsieh, C.-L., Abiona, O., … McLellan, J. S. (2020). Cryo-EM Structure of the 2019-nCoV Spike in the Prefusion Conformation. BioRxiv : The Preprint Server for Biology. https://doi.org/10.1101/2020.02.11.944462

    Walls, A. C., Park, Y. J., Tortorici, M. A., Wall, A., McGuire, A. T., & Veesler, D. (2020). Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell, 181(2), 281-292.e6. https://doi.org/10.1016/j.cell.2020.02.058

    Lan, J., Ge, J., Yu, J., Shan, S., Zhou, H., Fan, S., … Wang, X. (2020). Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature, 581(7807), 215–220. https://doi.org/10.1038/s41586-020-2180-5